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  • Promoterless (lowest background)
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Reporter systems

  • Fluorescent protein promoter reporters
    • Promoterless (lowest background)
    • Promoterless (traditional)
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Fluorescent protein promoter reporters: on-demand reporting

On-demand reporter vectors are the next generation of promoter reporters. With these reporter systems, you can compensate effectively for reporter background without compromising your assay’s signal intensity. Low background and a bright signal are no longer mutually exclusive.

On-demand reporter vectors are the next generation of promoter reporters. With these reporter systems, you can compensate effectively for reporter background without compromising your assay’s signal intensity. Low background and a bright signal are no longer mutually exclusive.

The challenges: overcoming high background & low signal intensity

Traditional promoter reporter assays generally struggle with the fact that most promoters are not very “tight”. As a result, your promoter of interest may drive reporter expression even without being activated—for example, during the time between transfection and the start of your experiment. These preexisting reporter molecules (the background) are the main cause of a low signal-to-noise ratio after promoter induction during the actual experiment.

One previous approach to this problem was to modify reporters for very quick, constitutive degradation. However, because these reporters are constitutively degraded as soon as they are made, it is impossible to accumulate a large quantity of reporter molecules inside the cell, even upon promoter activation. As a result, only a fraction of the reporter molecules are present long enough to be measured, and this type of assay has low signal intensity.

The solution: reporters on demand

The On-Demand Living Colors Fluorescent Protein Reporter Systems meet the challenge by providing both a low background and a broad dynamic range. This versatility is possible because they use a combination of technologies: each system includes a bright fluorescent protein reporter (AmCyan1, tdTomato, or ZsGreen1) for high signal intensity, coupled with ligand-dependent ProteoTuner protein stabilization/destabilization technology to eliminate background.

In these systems, the fluorescent protein reporter is expressed as a fusion protein tagged on its N-terminus with a ligand-dependent destabilization domain (DD). The DD rapidly targets the reporter protein for proteasomal degradation, guaranteeing a low reporter background signal at the start of your experiment. However, when the small, membrane-permeant ligand Shield1 is added to the sample, it binds to the DD and protects the reporter from degradation, so that it can accumulate.

By adding Shield1 simultaneously with your candidate inducer, you can effectively stabilize the reporter protein when it is synthesized in response to promoter activation. The majority of the fluorescent protein reporter molecules expressed during promoter activation will contribute to your readout, allowing for a considerably higher dynamic range and drastically improved signal-to-noise ratio compared to other types of reporter systems.

On-demand fluorescent protein reporter systems Traditional reporter systems
Background Uniformly low Promoter-dependent; may be high
Signal Bright Reporter-dependent. If background is low, signal is usually dim
Signal-to-noise ratio High, due to bright signal and low background Often low, especially when background is low
Studying timely promoter activity by eliminating unwanted reporter molecules Easy—simply remove Shield1 reagent Difficult; depends on reporter's natural lifespan

High signal, low background

In order to demonstrate the high signal-to-noise ratio and wide dynamic range of the DD fluorescent protein reporter systems, we compared the fold induction achieved using the DD-fluorescent protein reporters with that achieved using regular (non-destabilized) fluorescent proteins. The DD-tagged reporters stabilized by Shield1 had a much wider dynamic range, and therefore a much larger fold increase in the signal than the untagged versions of the same reporters. For the untagged versions, we observed high background fluorescence from reporter molecules that accumulated prior to induction, which drastically reduced the fold increase in signal intensity.

Choose your on-demand reporter system

Our on-demand reporter systems each consist of the necessary vectors (red, green, or cyan) plus Shield1.

Flexible choices

Use the DD fluorescent protein reporter systems to monitor any promoter of interest—just insert your promoter of interest upstream of the DD reporter. Choose from plasmid or lentiviral vector formats.

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Cat. # Product Size License Quantity Details
632192 DD-ZsGreen1 Reporter System Each USD $569.00

License Statement

ID Number  
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.

The DD-ZsGreen1 Reporter System includes the pDD-ZsGreen1 Reporter vector and Shield1. The pDD-ZsGreen1 Reporter is a promoterless vector designed to insert your promoter of interest upstream of the green fluorescent protein ZsGreen1, tagged at its N-terminus with the ProteoTuner destabilization domain (DD). The DD causes the reporter protein to be rapidly targeted to and degraded by proteasomes. This very efficient and controllable destabilization method will minimize any reporter background fluorescence from leaky promoters prior to promoter activation.

To analyze promoter activity, a candidate inducer is added to the medium along with Shield1, which effectively stabilizes the reporter protein and allows it to accumulate. As a result, only the reporter molecules expressed during promoter induction will contribute to the fluorescence signal, providing a considerably higher signal-to-noise ratio than that obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

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DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

632191 DD-AmCyan1 Reporter System Each USD $569.00

License Statement

ID Number  
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.

The DD-AmCyan1 Reporter System includes the pDD-AmCyan1 Reporter vector and Shield1. The pDD-AmCyan1 Reporter is a promoterless vector that allows you to insert your promoter of interest upstream of the cyan fluorescent protein AmCyan1, tagged at its N-terminus with the ProteoTuner destabilization domain (DD). The DD causes the reporter protein to be rapidly targeted to and degraded by proteasomes. This very efficient and controllable destabilization method will minimize any reporter background fluorescence from leaky promoters prior to promoter activation.

To analyze promoter activity, a candidate inducer is added to the medium along with Shield1, which effectively stabilizes the reporter protein and allows it to accumulate. As a result, only the reporter molecules expressed during promoter induction will contribute to the fluorescence signal, providing a considerably higher signal-to-noise ratio than that obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

632190 DD-tdTomato Reporter System Each USD $569.00

License Statement

ID Number  
72 Living Colors Fluorescent Protein Products:

Not-For-Profit Entities: Orders may be placed in the normal manner by contacting your local representative or Takara Bio USA, Inc. Customer Service. Any and all uses of this product will be subject to the terms and conditions of the Non-Commercial Use License Agreement (the “Non-Commercial License”), a copy of which can be found below. As a condition of sale of this product to you, and prior to using this product, you must agree to the terms and conditions of the Non-Commercial License. Under the Non-Commercial License, Takara Bio USA, Inc. grants Not-For-Profit Entities a non-exclusive, non-transferable, non-sublicensable and limited license to use this product for internal, non-commercial scientific research use only. Such license specifically excludes the right to sell or otherwise transfer this product, its components or derivatives thereof to third parties. No modifications to the product may be made without express written permission from Takara Bio USA, Inc. Any other use of this product requires a different license from Takara Bio USA, Inc. For license information, please contact a licensing representative by phone at 650.919.7320 or by e-mail at licensing@takarabio.com.

For-Profit Entities wishing to use this product are required to obtain a license from Takara Bio USA, Inc. For license information, please contact a licensing representative by e-mail at licensing@takarabio.com.

Not-For-Profit Non-Commercial Use License:
A copy of the DD-tdTomato Reporter System product License Agreement can be found by clicking here.
44 The DsRed-Monomer and the Fruit Fluorescent Proteins are covered by one or more of the following U.S. Patents: 7,671,185, 7,9110,714 and 8,664,471.
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.
69 The DsRed-Monomer, DsRed Express, E2-Crimson and the Fruit Fluorescent Proteins are covered by one or more of the following U.S. Patents: 7,250,298; 7,671,185; 7,910,714; 8,664,471 and 8,679,749.

The DD-tdTomato Reporter System includes the pDD-tdTomato Reporter vector and Shield1. The pDD-tdTomato Reporter is a promoterless vector that allows you to insert your promoter of interest upstream of the red fluorescent protein tdTomato, tagged at its N-terminus with the ProteoTuner destabilization domain (DD). The DD causes the reporter protein to be rapidly targeted to and degraded by proteasomes. This very efficient and controllable destabilization method will minimize background fluorescence from leaky promoters prior to promoter activation.

To analyze promoter activity, a candidate inducer is added to the medium along with Shield1, which effectively stabilizes the reporter protein and allows it to accumulate. As a result, only the reporter molecules expressed during promoter induction will contribute to the fluorescence signal, providing a considerably higher signal-to-noise ratio than that obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components You May Also Like Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model. False-color overlay images (regions of interest encircled) indicate that the imaging system could detect tdTomato fluorescence in the cadaver model, but not GFP fluorescence. Panel A. Implanted tube with 100 x 106 MDA-MB-231-tdTomato-expressing cells, imaged with the DsRed filter set. Exposure time: 1 sec. Panel B. Implanted tube with 100 x 106 MDA-MB-231-GFP-expressing cells, imaged with the GFP filter set. Exposure time: 1 sec.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

631753 Lenti-X™ DD Red Reporter System Each USD $1096.00

License Statement

ID Number  
63 Use of this product is covered by one or more of the following U.S. Patent Nos. and corresponding patent claims outside the U.S.: 6,998,115; 7,427,394. This product is intended for research purposes only. It may not be used for (i) any human or veterinary use, including without limitation therapeutic and prophylactic use, (ii) any clinical use, including without limitation diagnostic use, (iii) screening of chemical and/or biological compounds for the identification of pharmaceutically active agents (including but not limited to screening of small molecules), target validation, preclinical testing services, or drug development. Any use of this product for any of the above mentioned purposes requires a license from the Massachusetts Institute of Technology.
72 Living Colors Fluorescent Protein Products:

Not-For-Profit Entities: Orders may be placed in the normal manner by contacting your local representative or Takara Bio USA, Inc. Customer Service. Any and all uses of this product will be subject to the terms and conditions of the Non-Commercial Use License Agreement (the “Non-Commercial License”), a copy of which can be found below. As a condition of sale of this product to you, and prior to using this product, you must agree to the terms and conditions of the Non-Commercial License. Under the Non-Commercial License, Takara Bio USA, Inc. grants Not-For-Profit Entities a non-exclusive, non-transferable, non-sublicensable and limited license to use this product for internal, non-commercial scientific research use only. Such license specifically excludes the right to sell or otherwise transfer this product, its components or derivatives thereof to third parties. No modifications to the product may be made without express written permission from Takara Bio USA, Inc. Any other use of this product requires a different license from Takara Bio USA, Inc. For license information, please contact a licensing representative by phone at 650.919.7320 or by e-mail at licensing@takarabio.com.

For-Profit Entities wishing to use this product are required to obtain a license from Takara Bio USA, Inc. For license information, please contact a licensing representative by e-mail at licensing@takarabio.com.

Not-For-Profit Non-Commercial Use License:
A copy of the Lenti-X™ DD Red Reporter System product License Agreement can be found by clicking here.
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.
55 cPPT Element. This product and its use are the subject to one or more of the following U.S. Pat. No. 8,093,042. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The buyer cannot disclose information, sell or otherwise transfer this product, its components or materials made using this product or its components to a third party or otherwise use this product or its components or materials made using this product or its components for any commercial purposes. If the buyer is not willing to accept the limitations of this limited use statement, Takara Bio USA, Inc. is willing to accept return of the product with a full refund. For information on purchasing a license to the DNA-Flap technology for purposes other than research, contact the Transfer of Technology Office, Institut Pasteur, 28 rue du Docteur Roux, 75 724 Paris Cedex 15 (www.pasteur.fr).
42 Use of the Tetracycline controllable expression systems (the "Tet Technology") is covered by a series of patents including U.S. Patent # 8383364, # 9181556 , European patents EP # 1954811, #2352833 and corresponding patent claims outside these regions which are proprietary to TET Systems GmbH & Co. KG. Academic research institutions are granted an automatic license with the purchase of this product to use the Tet Technology only for internal, academic research purposes, which license specifically excludes the right to sell, or otherwise transfer, the Tet Technology or its component parts to third parties. Notwithstanding the above, academic and not-for profit research institutions whose research using the Tet Technology is sponsored by for profit organizations, which shall receive ownership to any data and results stemming from the sponsored research, shall need a commercial license agreement from TET Systems in order to use the Tet Technology. In accepting this license, all users acknowledge that the Tet Technology is experimental in nature. TET Systems GmbH & Co. KG makes no warranties, express or implied or of any kind, and hereby disclaims any warranties, representations, or guarantees of any kind as to the Tet Technology, patents, or products. All others are invited to request a license from TET Systems GmbH & Co. KG prior to purchasing these reagents or using them for any purpose. Takara Bio USA, Inc. is required by its licensing agreement to submit a report of all purchasers of the Tet-controllable expression system to TET Systems.

For license information, please contact:
GSF/CEO
TET Systems GmbH & Co. KG,
Im Neuenheimer Feld 582
69120 Heidelberg
Germany
Tel: +49 6221 5880400
Fax: +49 6221 5880404
email: info@tetsystems.com
or use the electronic licensing request form via http://www.tetsystems.com/ip-licensing/licensing/for-profit-research
44 The DsRed-Monomer and the Fruit Fluorescent Proteins are covered by one or more of the following U.S. Patents: 7,671,185, 7,9110,714 and 8,664,471.
69 The DsRed-Monomer, DsRed Express, E2-Crimson and the Fruit Fluorescent Proteins are covered by one or more of the following U.S. Patents: 7,250,298; 7,671,185; 7,910,714; 8,664,471 and 8,679,749.
K11 This product and its use are the subject to one or more of the following U.S. Pat. 8,093,042 and foreign equivalents. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and com­ponents of the product in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The buyer cannot disclose information, sell or otherwise transfer this product, its components or materials made using this product or its components to a third party or otherwise use this product or its components or materials made using this product or its components for any com­mercial purposes. If the buyer is not willing to accept the limitations of this limited use statement, Takara Bio USA is willing to accept return of the product with a full refund. For information on purchasing a license to the DNA-Flap technology for purposes other than research, contact the Transfer of Technology Office, Institut Pasteur, 28 rue du Docteur Roux, 75 724 Paris Cedex 15 (www.pasteur.fr).

The Lenti-X DD Red Reporter System includes the Lenti-X DD-tdTomato Vector Set and Shield1. The Lenti-X DD-tdTomato Vector Set includes two lentiviral expression vectors (a reporter vector and a control vector) that produce high titers of recombinant lentivirus, which can efficiently transduce both dividing and nondividing mammalian cells. The system provides enough reagents for 16 packaging reactions. The pLVX-DD-tdTomato Reporter Vector is a promoterless vector that allows you to insert your promoter of interest upstream of the red fluorescent protein tdTomato, tagged at its N-terminus with the ProteoTuner destabilization domain (DD). In the absence of the membrane-permeant ligand Shield1, the DD causes the reporter protein to be rapidly targeted to and degraded by proteasomes. This very efficient and controllable destabilization method minimizes reporter background fluorescence from leaky promoters prior to promoter activation. To analyze promoter activity, a candidate inducer is added to the medium along with Shield1, which binds to the DD tag and thereby stabilizes the reporter protein and allows it to accumulate. As a result, only the reporter molecules expressed during promoter induction will contribute to the fluorescence signal, providing a considerably higher signal-to-noise ratio than that obtained with nondestabilized or constitutively destabilized reporter systems. Cells used to monitor uninduced promoters (e.g., the negative control) will be treated with Shield1 alone.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components You May Also Like Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model. False-color overlay images (regions of interest encircled) indicate that the imaging system could detect tdTomato fluorescence in the cadaver model, but not GFP fluorescence. Panel A. Implanted tube with 100 x 106 MDA-MB-231-tdTomato-expressing cells, imaged with the DsRed filter set. Exposure time: 1 sec. Panel B. Implanted tube with 100 x 106 MDA-MB-231-GFP-expressing cells, imaged with the GFP filter set. Exposure time: 1 sec.

Back

Lenti-X reporter systems are ideal for your studies with limited numbers of cells

Lenti-X reporter systems are ideal for your studies with limited numbers of cells

Lenti-X reporter systems are ideal for your studies with limited numbers of cells (e.g., stem cells), or to study multiple promoter activation cycles and/or time points, in order to produce many sets of data over time. Choose systems with secreted luciferase or with on-demand fluorescent reporters.

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Lenti-X chemiluminescent and fluorescent reporter vectors

Lenti-X chemiluminescent and fluorescent reporter vectors
Lenti-X chemiluminescent (Panel A) and fluorescent (Panel B) reporter vectors. Lenti-X vectors contain sequence elements that facilitate lentiviral packaging and/or boost expression of your reporter, including the LTRs, packaging signal (Ψ), Rev response element (RRE), and central polypurine tract/central termination sequence (cPPT/CTS) from HIV-1; and the woodchuck hepatitis virus post-transcriptional regulatory element (WPRE). MetLuc = Metridia luciferase. DD = ligand-dependent destabilization domain. FP = fluorescent protein (AmCyan1, ZsGreen1, or tdTomato).

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Lenti-X reporter systems provide low background and high signal intensity

Lenti-X reporter systems provide low background and high signal intensity

Lenti-X reporter systems provide low background and high signal intensity. HEK 293 cells were transduced with pLVX-CRE-MetLuc Reporter Vector (Panel A) or pLVX-CRE-DD-ZsGreen1 Reporter Vector (Panel B), treated with forskolin, and assayed according to the respective protocols. RLU = relative light units. RFU = relative fluorescence units.

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Lentiviral on-demand fluorescent reporter vectors

Lentiviral on-demand fluorescent reporter vectors

Lentiviral on-demand fluorescent reporter vectors. Lenti-X vectors contain sequence elements that facilitate lentiviral packaging and/or boost expression of your reporter, including the LTRs, packaging signal (Ψ), Rev response element (RRE), and central polypurine tract/central termination sequence (cPPT/CTS) from HIV-1; and the woodchuck hepatitis virus post-transcriptional regulatory element (WPRE). DD = ligand-dependent destabilization domain. FP = fluorescent protein (AmCyan1, ZsGreen1, or tdTomato).

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

631751 Lenti-X™ DD Green Reporter System Each USD $1096.00

License Statement

ID Number  
63 Use of this product is covered by one or more of the following U.S. Patent Nos. and corresponding patent claims outside the U.S.: 6,998,115; 7,427,394. This product is intended for research purposes only. It may not be used for (i) any human or veterinary use, including without limitation therapeutic and prophylactic use, (ii) any clinical use, including without limitation diagnostic use, (iii) screening of chemical and/or biological compounds for the identification of pharmaceutically active agents (including but not limited to screening of small molecules), target validation, preclinical testing services, or drug development. Any use of this product for any of the above mentioned purposes requires a license from the Massachusetts Institute of Technology.
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.
55 cPPT Element. This product and its use are the subject to one or more of the following U.S. Pat. No. 8,093,042. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The buyer cannot disclose information, sell or otherwise transfer this product, its components or materials made using this product or its components to a third party or otherwise use this product or its components or materials made using this product or its components for any commercial purposes. If the buyer is not willing to accept the limitations of this limited use statement, Takara Bio USA, Inc. is willing to accept return of the product with a full refund. For information on purchasing a license to the DNA-Flap technology for purposes other than research, contact the Transfer of Technology Office, Institut Pasteur, 28 rue du Docteur Roux, 75 724 Paris Cedex 15 (www.pasteur.fr).
42 Use of the Tetracycline controllable expression systems (the "Tet Technology") is covered by a series of patents including U.S. Patent # 8383364, # 9181556 , European patents EP # 1954811, #2352833 and corresponding patent claims outside these regions which are proprietary to TET Systems GmbH & Co. KG. Academic research institutions are granted an automatic license with the purchase of this product to use the Tet Technology only for internal, academic research purposes, which license specifically excludes the right to sell, or otherwise transfer, the Tet Technology or its component parts to third parties. Notwithstanding the above, academic and not-for profit research institutions whose research using the Tet Technology is sponsored by for profit organizations, which shall receive ownership to any data and results stemming from the sponsored research, shall need a commercial license agreement from TET Systems in order to use the Tet Technology. In accepting this license, all users acknowledge that the Tet Technology is experimental in nature. TET Systems GmbH & Co. KG makes no warranties, express or implied or of any kind, and hereby disclaims any warranties, representations, or guarantees of any kind as to the Tet Technology, patents, or products. All others are invited to request a license from TET Systems GmbH & Co. KG prior to purchasing these reagents or using them for any purpose. Takara Bio USA, Inc. is required by its licensing agreement to submit a report of all purchasers of the Tet-controllable expression system to TET Systems.

For license information, please contact:
GSF/CEO
TET Systems GmbH & Co. KG,
Im Neuenheimer Feld 582
69120 Heidelberg
Germany
Tel: +49 6221 5880400
Fax: +49 6221 5880404
email: info@tetsystems.com
or use the electronic licensing request form via http://www.tetsystems.com/ip-licensing/licensing/for-profit-research
K11 This product and its use are the subject to one or more of the following U.S. Pat. 8,093,042 and foreign equivalents. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and com­ponents of the product in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The buyer cannot disclose information, sell or otherwise transfer this product, its components or materials made using this product or its components to a third party or otherwise use this product or its components or materials made using this product or its components for any com­mercial purposes. If the buyer is not willing to accept the limitations of this limited use statement, Takara Bio USA is willing to accept return of the product with a full refund. For information on purchasing a license to the DNA-Flap technology for purposes other than research, contact the Transfer of Technology Office, Institut Pasteur, 28 rue du Docteur Roux, 75 724 Paris Cedex 15 (www.pasteur.fr).

The Lenti-X DD Green Reporter System includes the Lenti-X DD-ZsGreen1 Vector Set and Shield1. The Lenti-X DD-ZsGreen1 Vector Set includes two lentiviral expression vectors (a reporter vector and a control vector) that produce high titers of recombinant lentivirus, which can efficiently transduce both dividing and nondividing mammalian cells. The system provides enough reagents for 16 packaging reactions. The pLVX-DD-ZsGreen1 Reporter Vector is a promoterless vector that allows you to insert your promoter of interest upstream of the green fluorescent protein ZsGreen1, tagged at its N-terminus with the ProteoTuner destabilization domain (DD). In the absence of the membrane-permeant ligand Shield1, the DD causes the reporter protein to be rapidly targeted to and degraded by proteasomes. This very efficient and controllable destabilization method minimizes reporter background fluorescence from leaky promoters prior to promoter activation. To analyze promoter activity, a candidate inducer is added to the medium along with Shield1, which binds to the DD tag and thereby stabilizes the reporter protein and allows it to accumulate. As a result, only the reporter molecules expressed during promoter induction will contribute to the fluorescence signal, providing a considerably higher signal-to-noise ratio than that obtained with nondestabilized or constitutively destabilized reporter systems. Cells used to monitor uninduced promoters (e.g., the negative control) will be treated with Shield1 alone.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

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DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Lenti-X reporter systems are ideal for your studies with limited numbers of cells

Lenti-X reporter systems are ideal for your studies with limited numbers of cells

Lenti-X reporter systems are ideal for your studies with limited numbers of cells (e.g., stem cells), or to study multiple promoter activation cycles and/or time points, in order to produce many sets of data over time. Choose systems with secreted luciferase or with on-demand fluorescent reporters.

Back

Lenti-X chemiluminescent and fluorescent reporter vectors

Lenti-X chemiluminescent and fluorescent reporter vectors
Lenti-X chemiluminescent (Panel A) and fluorescent (Panel B) reporter vectors. Lenti-X vectors contain sequence elements that facilitate lentiviral packaging and/or boost expression of your reporter, including the LTRs, packaging signal (Ψ), Rev response element (RRE), and central polypurine tract/central termination sequence (cPPT/CTS) from HIV-1; and the woodchuck hepatitis virus post-transcriptional regulatory element (WPRE). MetLuc = Metridia luciferase. DD = ligand-dependent destabilization domain. FP = fluorescent protein (AmCyan1, ZsGreen1, or tdTomato).

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Lentiviral on-demand fluorescent reporter vectors

Lentiviral on-demand fluorescent reporter vectors

Lentiviral on-demand fluorescent reporter vectors. Lenti-X vectors contain sequence elements that facilitate lentiviral packaging and/or boost expression of your reporter, including the LTRs, packaging signal (Ψ), Rev response element (RRE), and central polypurine tract/central termination sequence (cPPT/CTS) from HIV-1; and the woodchuck hepatitis virus post-transcriptional regulatory element (WPRE). DD = ligand-dependent destabilization domain. FP = fluorescent protein (AmCyan1, ZsGreen1, or tdTomato).

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

631748 Lenti-X™ DD Cyan Reporter System Each USD $1096.00

License Statement

ID Number  
63 Use of this product is covered by one or more of the following U.S. Patent Nos. and corresponding patent claims outside the U.S.: 6,998,115; 7,427,394. This product is intended for research purposes only. It may not be used for (i) any human or veterinary use, including without limitation therapeutic and prophylactic use, (ii) any clinical use, including without limitation diagnostic use, (iii) screening of chemical and/or biological compounds for the identification of pharmaceutically active agents (including but not limited to screening of small molecules), target validation, preclinical testing services, or drug development. Any use of this product for any of the above mentioned purposes requires a license from the Massachusetts Institute of Technology.
55 cPPT Element. This product and its use are the subject to one or more of the following U.S. Pat. No. 8,093,042. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The buyer cannot disclose information, sell or otherwise transfer this product, its components or materials made using this product or its components to a third party or otherwise use this product or its components or materials made using this product or its components for any commercial purposes. If the buyer is not willing to accept the limitations of this limited use statement, Takara Bio USA, Inc. is willing to accept return of the product with a full refund. For information on purchasing a license to the DNA-Flap technology for purposes other than research, contact the Transfer of Technology Office, Institut Pasteur, 28 rue du Docteur Roux, 75 724 Paris Cedex 15 (www.pasteur.fr).
42 Use of the Tetracycline controllable expression systems (the "Tet Technology") is covered by a series of patents including U.S. Patent # 8383364, # 9181556 , European patents EP # 1954811, #2352833 and corresponding patent claims outside these regions which are proprietary to TET Systems GmbH & Co. KG. Academic research institutions are granted an automatic license with the purchase of this product to use the Tet Technology only for internal, academic research purposes, which license specifically excludes the right to sell, or otherwise transfer, the Tet Technology or its component parts to third parties. Notwithstanding the above, academic and not-for profit research institutions whose research using the Tet Technology is sponsored by for profit organizations, which shall receive ownership to any data and results stemming from the sponsored research, shall need a commercial license agreement from TET Systems in order to use the Tet Technology. In accepting this license, all users acknowledge that the Tet Technology is experimental in nature. TET Systems GmbH & Co. KG makes no warranties, express or implied or of any kind, and hereby disclaims any warranties, representations, or guarantees of any kind as to the Tet Technology, patents, or products. All others are invited to request a license from TET Systems GmbH & Co. KG prior to purchasing these reagents or using them for any purpose. Takara Bio USA, Inc. is required by its licensing agreement to submit a report of all purchasers of the Tet-controllable expression system to TET Systems.

For license information, please contact:
GSF/CEO
TET Systems GmbH & Co. KG,
Im Neuenheimer Feld 582
69120 Heidelberg
Germany
Tel: +49 6221 5880400
Fax: +49 6221 5880404
email: info@tetsystems.com
or use the electronic licensing request form via http://www.tetsystems.com/ip-licensing/licensing/for-profit-research
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.
K11 This product and its use are the subject to one or more of the following U.S. Pat. 8,093,042 and foreign equivalents. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and com­ponents of the product in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The buyer cannot disclose information, sell or otherwise transfer this product, its components or materials made using this product or its components to a third party or otherwise use this product or its components or materials made using this product or its components for any com­mercial purposes. If the buyer is not willing to accept the limitations of this limited use statement, Takara Bio USA is willing to accept return of the product with a full refund. For information on purchasing a license to the DNA-Flap technology for purposes other than research, contact the Transfer of Technology Office, Institut Pasteur, 28 rue du Docteur Roux, 75 724 Paris Cedex 15 (www.pasteur.fr).

The Lenti-X DD Cyan Reporter System includes the Lenti-X DD-AmCyan1 Vector Set and Shield1. The Lenti-X DD-AmCyan1 Vector Set includes two lentiviral expression vectors (a reporter vector and a control vector) that produce high titers of recombinant lentivirus, which can efficiently transduce both dividing and nondividing mammalian cells. The system provides enough reagents for 16 packaging reactions. The pLVX-DD-AmCyan1 Reporter Vector is a promoterless vector that allows you to insert your promoter of interest upstream of the cyan fluorescent protein AmCyan1, tagged at its N-terminus with the ProteoTuner destabilization domain (DD). In the absence of the membrane-permeant ligand Shield1, the DD causes the reporter protein to be rapidly targeted to and degraded by proteasomes. This very efficient and controllable destabilization method minimizes reporter background fluorescence from leaky promoters prior to promoter activation.To analyze promoter activity, a candidate inducer is added to the medium along with Shield1, which binds to the DD tag and thereby stabilizes the reporter protein and allows it to accumulate. As a result, only the reporter molecules expressed during promoter induction will contribute to the fluorescence signal, providing a considerably higher signal-to-noise ratio than that obtained with nondestabilized or constitutively destabilized reporter systems. Cells used to monitor uninduced promoters (e.g., the negative control) will be treated with Shield1 alone.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Lenti-X reporter systems are ideal for your studies with limited numbers of cells

Lenti-X reporter systems are ideal for your studies with limited numbers of cells

Lenti-X reporter systems are ideal for your studies with limited numbers of cells (e.g., stem cells), or to study multiple promoter activation cycles and/or time points, in order to produce many sets of data over time. Choose systems with secreted luciferase or with on-demand fluorescent reporters.

Back

Lenti-X chemiluminescent and fluorescent reporter vectors

Lenti-X chemiluminescent and fluorescent reporter vectors
Lenti-X chemiluminescent (Panel A) and fluorescent (Panel B) reporter vectors. Lenti-X vectors contain sequence elements that facilitate lentiviral packaging and/or boost expression of your reporter, including the LTRs, packaging signal (Ψ), Rev response element (RRE), and central polypurine tract/central termination sequence (cPPT/CTS) from HIV-1; and the woodchuck hepatitis virus post-transcriptional regulatory element (WPRE). MetLuc = Metridia luciferase. DD = ligand-dependent destabilization domain. FP = fluorescent protein (AmCyan1, ZsGreen1, or tdTomato).

Back

Lentiviral on-demand fluorescent reporter vectors

Lentiviral on-demand fluorescent reporter vectors

Lentiviral on-demand fluorescent reporter vectors. Lenti-X vectors contain sequence elements that facilitate lentiviral packaging and/or boost expression of your reporter, including the LTRs, packaging signal (Ψ), Rev response element (RRE), and central polypurine tract/central termination sequence (cPPT/CTS) from HIV-1; and the woodchuck hepatitis virus post-transcriptional regulatory element (WPRE). DD = ligand-dependent destabilization domain. FP = fluorescent protein (AmCyan1, ZsGreen1, or tdTomato).

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

631089 CRE DD Cyan Reporter System Each USD $569.00

License Statement

ID Number  
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.

The CRE DD Cyan Reporter System is designed to monitor cAMP response element binding protein (CREB) activity in mammalian cells, with minimal background signal. It includes the pCRE-DD-AmCyan1 Reporter vector and Shield1.

pCRE-DD-AmCyan1 encodes a cyan fluorescent protein reporter tagged at its N-terminus with the ProteoTuner destabilization domain (DD), and under the control of the CRE promoter. The DD causes the DD-AmCyan1 reporter to be rapidly targeted to and degraded by proteasomes. This minimizes background fluorescence from leaky promoters prior to promoter activation.

To monitor CREB activity, a candidate inducer is added to the medium simultaneously with the DD's stabilizing ligand, Shield1. This allows DD-AmCyan1 to accumulate in response to CREB activation. As a result, only the reporter molecules expressed during CRE induction contribute to the fluorescence signal. This system provides a considerably higher signal-to-noise ratio than can be obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

631087 CRE DD Red Reporter System Each USD $569.00

License Statement

ID Number  
44 The DsRed-Monomer and the Fruit Fluorescent Proteins are covered by one or more of the following U.S. Patents: 7,671,185, 7,9110,714 and 8,664,471.
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.
72 Living Colors Fluorescent Protein Products:

Not-For-Profit Entities: Orders may be placed in the normal manner by contacting your local representative or Takara Bio USA, Inc. Customer Service. Any and all uses of this product will be subject to the terms and conditions of the Non-Commercial Use License Agreement (the “Non-Commercial License”), a copy of which can be found below. As a condition of sale of this product to you, and prior to using this product, you must agree to the terms and conditions of the Non-Commercial License. Under the Non-Commercial License, Takara Bio USA, Inc. grants Not-For-Profit Entities a non-exclusive, non-transferable, non-sublicensable and limited license to use this product for internal, non-commercial scientific research use only. Such license specifically excludes the right to sell or otherwise transfer this product, its components or derivatives thereof to third parties. No modifications to the product may be made without express written permission from Takara Bio USA, Inc. Any other use of this product requires a different license from Takara Bio USA, Inc. For license information, please contact a licensing representative by phone at 650.919.7320 or by e-mail at licensing@takarabio.com.

For-Profit Entities wishing to use this product are required to obtain a license from Takara Bio USA, Inc. For license information, please contact a licensing representative by e-mail at licensing@takarabio.com.

Not-For-Profit Non-Commercial Use License:
A copy of the CRE DD Red Reporter System product License Agreement can be found by clicking here.

The CRE DD Red Reporter System is designed to monitor cAMP response element binding protein (CREB) activity in mammalian cells, with minimal background signal. It includes the pCRE-DD-tdTomato Reporter vector and Shield1.

pCRE-DD-tdTomato encodes a red fluorescent protein reporter tagged at its N-terminus with the ProteoTuner destabilization domain (DD), and under the control of the CRE promoter. The DD causes the DD-tdTomato reporter to be rapidly targeted to and degraded by proteasomes. This minimizes background fluorescence from leaky promoters prior to promoter activation.

To monitor CREB activity, a candidate inducer is added to the medium simultaneously with the DD's stabilizing ligand, Shield1. This allows DD-tdTomato to accumulate in response to CREB activation. As a result, only the reporter molecules expressed during CRE induction contribute to the fluorescence signal. This system provides a considerably higher signal-to-noise ratio than can be obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model. False-color overlay images (regions of interest encircled) indicate that the imaging system could detect tdTomato fluorescence in the cadaver model, but not GFP fluorescence. Panel A. Implanted tube with 100 x 106 MDA-MB-231-tdTomato-expressing cells, imaged with the DsRed filter set. Exposure time: 1 sec. Panel B. Implanted tube with 100 x 106 MDA-MB-231-GFP-expressing cells, imaged with the GFP filter set. Exposure time: 1 sec.

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Lenti-X reporter systems provide low background and high signal intensity

Lenti-X reporter systems provide low background and high signal intensity

Lenti-X reporter systems provide low background and high signal intensity. HEK 293 cells were transduced with pLVX-CRE-MetLuc Reporter Vector (Panel A) or pLVX-CRE-DD-ZsGreen1 Reporter Vector (Panel B), treated with forskolin, and assayed according to the respective protocols. RLU = relative light units. RFU = relative fluorescence units.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

631085 CRE DD Green Reporter System Each USD $569.00

License Statement

ID Number  
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.

The CRE DD Green Reporter System is designed to monitor cAMP response element binding protein (CREB) activity in mammalian cells, with minimal background signal. It includes the pCRE-DD-ZsGreen1 Reporter vector and Shield1.

pCRE-DD-ZsGreen1 encodes a green fluorescent protein reporter tagged at its N-terminus with the ProteoTuner destabilization domain (DD), and under the control of the CRE promoter. The DD causes the DD-ZsGreen1 reporter to be rapidly targeted to and degraded by proteasomes. This minimizes background fluorescence from leaky promoters prior to promoter activation.

To monitor CREB activity, a candidate inducer is added to the medium simultaneously with the DD's stabilizing ligand, Shield1. This allows DD-ZsGreen1 to accumulate in response to CREB activation. As a result, only the reporter molecules expressed during CRE induction contribute to the fluorescence signal. This system provides a considerably higher signal-to-noise ratio than can be obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

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631085: CRE DD Green Reporter System

631085: CRE DD Green Reporter System
631083 NFkappaB DD Cyan Reporter System Each USD $569.00

License Statement

ID Number  
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.

The NFkB DD Cyan Reporter System is designed to monitor NFkB activation in mammalian cells, with minimal background signal. It includes the pNFkB-DD-AmCyan1 Reporter vector and Shield1.

pNFkB-DD-AmCyan1 encodes a cyan fluorescent protein reporter tagged at its N-terminus with the ProteoTuner destabilization domain (DD), and under the control of the NFkB promoter. The DD causes the DD-AmCyan1 reporter to be rapidly targeted to and degraded by proteasomes. This minimizes background signal from leaky promoters prior to promoter activation.

To monitor NFkB activity, a candidate inducer is added to the medium simultaneously with the DD's stabilizing ligand, Shield1. This allows DD-AmCyan1 to accumulate in response to NFkB activation. As a result, only the reporter molecules expressed during NFkB induction contribute to the fluorescence signal. This system provides a considerably higher signal-to-noise ratio than can be obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

631081 NFkappaB DD Red Reporter System Each USD $569.00

License Statement

ID Number  
44 The DsRed-Monomer and the Fruit Fluorescent Proteins are covered by one or more of the following U.S. Patents: 7,671,185, 7,9110,714 and 8,664,471.
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.
72 Living Colors Fluorescent Protein Products:

Not-For-Profit Entities: Orders may be placed in the normal manner by contacting your local representative or Takara Bio USA, Inc. Customer Service. Any and all uses of this product will be subject to the terms and conditions of the Non-Commercial Use License Agreement (the “Non-Commercial License”), a copy of which can be found below. As a condition of sale of this product to you, and prior to using this product, you must agree to the terms and conditions of the Non-Commercial License. Under the Non-Commercial License, Takara Bio USA, Inc. grants Not-For-Profit Entities a non-exclusive, non-transferable, non-sublicensable and limited license to use this product for internal, non-commercial scientific research use only. Such license specifically excludes the right to sell or otherwise transfer this product, its components or derivatives thereof to third parties. No modifications to the product may be made without express written permission from Takara Bio USA, Inc. Any other use of this product requires a different license from Takara Bio USA, Inc. For license information, please contact a licensing representative by phone at 650.919.7320 or by e-mail at licensing@takarabio.com.

For-Profit Entities wishing to use this product are required to obtain a license from Takara Bio USA, Inc. For license information, please contact a licensing representative by e-mail at licensing@takarabio.com.

Not-For-Profit Non-Commercial Use License:
A copy of the NFkappaB DD Red Reporter System product License Agreement can be found by clicking here.

The NFkB DD Red Reporter System is designed to monitor NFkB activation in mammalian systems, with minimal background signal. It includes the pNFkB-DD-tdTomato Reporter vector and Shield1.

pNFkB-DD-tdTomato encodes a red fluorescent protein reporter tagged at its N-terminus with the ProteoTuner destabilization domain (DD), and under the control of the NFkB promoter. The DD causes the DD-tdTomato reporter to be rapidly targeted to and degraded by proteasomes. This minimizes background fluorescence from leaky promoters prior to promoter activation.

To monitor NFkB activity, a candidate inducer is added to the medium simultaneously with the DD's stabilizing ligand, Shield1. This allows DD-tdTomato to accumulate in response to NFkB activation. As a result, only the reporter molecules expressed during NFkB induction contribute to the fluorescence signal. This system provides a considerably higher signal-to-noise ratio than can be obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model

tdTomato, but not GFP, can be detected in the SCID mouse cadaver phantom model. False-color overlay images (regions of interest encircled) indicate that the imaging system could detect tdTomato fluorescence in the cadaver model, but not GFP fluorescence. Panel A. Implanted tube with 100 x 106 MDA-MB-231-tdTomato-expressing cells, imaged with the DsRed filter set. Exposure time: 1 sec. Panel B. Implanted tube with 100 x 106 MDA-MB-231-GFP-expressing cells, imaged with the GFP filter set. Exposure time: 1 sec.

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Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

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631081: NFkappaB DD Red Reporter System

631081: NFkappaB DD Red Reporter System
631079 NFkappaB DD Green Reporter System Each USD $569.00

License Statement

ID Number  
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.

The NFkB DD Green Reporter System is designed to monitor NFkB activation in mammalian cells, with minimal background signal. It includes the pNFkB-DD-ZsGreen1 Reporter vector and Shield1.

pNFkB-DD-ZsGreen1 encodes a green fluorescent protein reporter tagged at its N-terminus with the ProteoTuner destabilization domain (DD), and under the control of the NFkB promoter. The DD causes the DD-ZsGreen1 reporter to be rapidly targeted to and degraded by proteasomes. This minimizes background signal from leaky promoters prior to promoter activation.

To monitor NFkB activity, a candidate inducer is added to the medium simultaneously with the DD's stabilizing ligand, Shield1. This allows DD-ZsGreen1 to accumulate in response to NFkB activation. As a result, only reporter molecules expressed during NFkB induction will contribute to the fluorescence signal. This system provides a considerably higher signal-to-noise ratio than can be obtained with non-destabilized or constitutively destabilized reporter systems.

Notice to purchaser

Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

Documents Components Image Data

Back

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD

DD-Fluorescent Protein promoter reporters provide a much greater fold increase in signal intensity than traditional fluorescent protein reporters, which do not contain the DD. HEK 293 cells were transfected with plasmids encoding the following reporters: CRE-tdTomato, CRE-DD-tdTomato, CRE-ZsGreen1, and CRE-DD-ZsGreen1. 24 hr later, the cells were stimulated with 10 μM forskolin and simultaneously treated with 1 μM Shield1. After 4.5 hr, fluorescence intensity was measured via flow cytometry, and fold induction was calculated. The tdTomato and ZsGreen1 reporters containing the DD had three- and six-fold greater fluorescence intensity respectively, than the versions without the DD, due to the latter’s increased background levels.

Back

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization

Ligand-dependent, targeted, and reversible fluorescent protein reporter stabilization. A small destabilization domain (DD) is fused to the fluorescent protein reporter. The small membrane-permeant ligand Shield1 binds to the DD and protects the entire fusion protein from proteasomal degradation. Removal of Shield1, however, causes rapid degradation of the entire DD-fluorescent protein reporter. The default pathway for the DD-Fluorescent Protein Reporter Systems is degradation of the DD-fluorescent protein reporter, assuring low background, unless Shield1 is present, assuring low background.

Back

631079: NFkappaB DD Green Reporter System

631079: NFkappaB DD Green Reporter System

Overview

  • The next generation of promoter reporters
  • High signal-to-noise ratio
  • Bright signal
  • Easy to monitor—red, green, and cyan options

More Information

Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.

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