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Shield1 ligand for protein stabilization Shield1 ligand
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Shield1 ligand for protein stabilization Shield1 ligand
Overviews Tet-One overview

ProteoTuner expression systems in plasmid format

Shield1-mediated control of protein expression

ProteoTuner plasmid expression systems allow for rapidly regulating the presence or absence of a protein of interest in your target cells. Clone your gene of interest in-frame with the destabilization domain tag (DD), either at the N or C terminus. In the absence of the Shield1 ligand in the culture medium, the DD-tagged fusion protein is immediately destabilized, but when Shield1 is added, the protein accumulates to detectable levels within 15–20 minutes.

ProteoTuner plasmid expression systems allow for rapidly regulating the presence or absence of a protein of interest in your target cells. Clone your gene of interest in-frame with the destabilization domain tag (DD), either at the N or C terminus. In the absence of the Shield1 ligand in the culture medium, the DD-tagged fusion protein is immediately destabilized, but when Shield1 is added, the protein accumulates to detectable levels within 15–20 minutes. Upon Shield1 removal, the halftime for the fusion protein's degradation can be as short as 30 minutes. Lentiviral and retroviral formats are also available.

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Cat. # Product Size License Quantity Details
632189 Shield1 500 uL USD $360.00

The Shield1 compound stabilizes a protein of interest tagged with the destabilization domain (DD), which is based on a mutated version of the FKBP protein. It is used to protect the DD fusion protein of interest from proteasomal degradation. The amount of Shield1 can be varied to tune the amount of stabilized protein of interest within the cell.

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 fusions exhibit predictable, dose-dependent protein stabilization by Shield1; using the DD optimal for your protein is crucial in getting the best performance

 DD fusions exhibit predictable, dose-dependent protein stabilization by Shield1; using the DD optimal for your protein is crucial in getting the best performance

DD fusions exhibit predictable, dose-dependent protein stabilization by Shield1; using the DD optimal for your protein is crucial in getting the best performance. While DD-N (solid blue line) is suitable for N-terminal fusions and even C-terminal fusions for many proteins, DD-C (dashed blue line) is optimal for C-terminal fusions and for those proteins that do not tolerate N-terminal fusions. HEK 293 cells expressing the DD fusions noted in the figure legend were treated with varying concentrations of Shield1. 12 hr later, the amount of AcGPF1 stabilized by different concentrations of Shield1 was detected by fluorescence intensity using flow cytometry. DD-C at the C-terminus of AcGFP showed a lower basal level of protein in the absence of Shield1 (purple line; see inset figure). MFI = mean fluorescence intensity.

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Structure of Shield1 stabilization ligand

Structure of Shield1 stabilization ligand
Structure of Shield1 stabilization ligand.

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Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization. A small destabilization domain (DD; blue) is fused to a target protein of interest. The small membrane-permeable ligand Shield1 (red) binds to the DD and protects it from proteasomal degradation. Removal of Shield1 however, causes rapid degradation of the entire fusion protein. The default pathway for the ProteoTuner systems is degradation of the fusion protein unless Shield1 is present.

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Protein stabilty controlled using the ProteoTuner shield system

Protein stabilty controlled using the ProteoTuner shield system

Protein stabilty controlled using the ProteoTuner shield system. DsRed-Express was cloned into pRetroX-PTuner IRES and used to infect HeLa cells. The amount of DD-tagged DsRed-Express stabilized by different concentrations of Shield1 was detected via Western blot using the Living Colors DsRed Polyclonal Antibody. Lane 1: molecular weight marker. Lane 2: 1X loading buffer. Lane 3: untreated HeLa cells (no virus, no Shield1). Lane 4: HeLa cells infected with the DD-DsRed Express construct; no Shield1. Lanes 5–8: HeLa cells infected with the DD-DsRed-Express construct and treated with 50, 250, 500, and 1,000 nM Shield1 respectively. Lane 9: 1X loading buffer. Lane 10: HEK 293 DsRed-Express stable cell line.

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632189: Shield1

632189: Shield1

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Control of actin stability with the ProteoTuner system

Control of actin stability with the ProteoTuner system

Control of actin stability with the ProteoTuner system. In the absence of Shield1, no DD-AcGFP1 is observed (Panel B) despite the presence of a normal actin filament network (Panel A). In the presence of Shield1, DD-AcGFP1 is stable and present in the actin network (Panel D).

632188 Shield1 5 mg USD $820.00

License Statement

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

After reconstitution in your solvent of choice, the Shield1 compound stabilizes a protein of interest tagged with the destabilization domain (DD), which is based on a mutated version of the FKBP protein. It is used to protect the DD fusion protein of interest from proteasomal degradation. The amount of Shield1 can be varied to tune the amount of the stabilized protein of interest in vivo.

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 fusions exhibit predictable, dose-dependent protein stabilization by Shield1; using the DD optimal for your protein is crucial in getting the best performance

 DD fusions exhibit predictable, dose-dependent protein stabilization by Shield1; using the DD optimal for your protein is crucial in getting the best performance

DD fusions exhibit predictable, dose-dependent protein stabilization by Shield1; using the DD optimal for your protein is crucial in getting the best performance. While DD-N (solid blue line) is suitable for N-terminal fusions and even C-terminal fusions for many proteins, DD-C (dashed blue line) is optimal for C-terminal fusions and for those proteins that do not tolerate N-terminal fusions. HEK 293 cells expressing the DD fusions noted in the figure legend were treated with varying concentrations of Shield1. 12 hr later, the amount of AcGPF1 stabilized by different concentrations of Shield1 was detected by fluorescence intensity using flow cytometry. DD-C at the C-terminus of AcGFP showed a lower basal level of protein in the absence of Shield1 (purple line; see inset figure). MFI = mean fluorescence intensity.

Back

Structure of Shield1 stabilization ligand

Structure of Shield1 stabilization ligand
Structure of Shield1 stabilization ligand.

Back

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization. A small destabilization domain (DD; blue) is fused to a target protein of interest. The small membrane-permeable ligand Shield1 (red) binds to the DD and protects it from proteasomal degradation. Removal of Shield1 however, causes rapid degradation of the entire fusion protein. The default pathway for the ProteoTuner systems is degradation of the fusion protein unless Shield1 is present.

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632188: Shield1

632188: Shield1
632172 ProteoTuner™ Shield System N Each USD $700.00

License Statement

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

Direct manipulation of the presence and absence of a specific protein of interest is a very powerful tool for analyzing protein function. The ProteoTuner Shield System N uses a unique method to regulate the amount of protein of interest present in a cell, quickly and directly. It utilizes a ligand-dependent destabilization domain (DD) and its membrane permeable stabilizing ligand, Shield1. The DD is based on a 12 kDa mutant of the FKBP protein, which is expressed as a tag onto the N-terminus of your protein of interest cloned into the pPTuner Vector. In the presence of Shield1, the DD-tagged protein is stabilized and will accumulate inside the cell. This ligand-dependent stabilization occurs very quickly, and has been observed as soon as 15–30 minutes after the addition of Shield1. However, in the absence of the protective ligand Shield1, the DD-tagged protein of interest is rapidly degraded. Removing the Shield1 (by splitting the cells into media without Shield1) allows for protein destabilization, causing a fast degradation of the protein of interest. The extent of stabilization via Shield1 directly correlates with the amount of the ligand in the medium, so it is possible to tune the amount of protein of interest present in the cell, by controlling the amount of the Shield1 ligand.

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 Resources

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Dose-dependent stabilization of DD-tagged AcGFP1 fluorescent protein

Dose-dependent stabilization of DD-tagged AcGFP1 fluorescent protein

Dose-dependent stabilization of DD-tagged AcGFP1 fluorescent protein. Cells were transfected with pDD-AcGFP1-PL, treated with the indicated amounts of Shield1, and the amount of stabilized DD-AcGFP1-PL was quantified by Western blot using the Living Colors A.v. Monoclonal Antibody(JL-8) to detect AcGFP1.

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Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization. A small destabilization domain (DD; blue) is fused to a target protein of interest. The small membrane-permeable ligand Shield1 (red) binds to the DD and protects it from proteasomal degradation. Removal of Shield1 however, causes rapid degradation of the entire fusion protein. The default pathway for the ProteoTuner systems is degradation of the fusion protein unless Shield1 is present.

Back

Predictable and reversible Shield1-dependent regulation of intracellular protein levels

Predictable and reversible Shield1-dependent regulation of intracellular protein levels

Predictable and reversible Shield1-dependent regulation of intracellular protein levels. NIH 3T3 cells stably expressing a DD-tagged yellow fluorescent protein were treated with varying concentrations of Shield1 over the course of one week, and samples of the population were assayed by flow cytometry at the indicated time points [Banaszynski, L. A., et al. (2006) Cell 126(5):995–1004].

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Shield1 results in predictable changes in cellular morphology

Shield1 results in predictable changes in cellular morphology

Shield1 results in predictable changes in cellular morphology. A constitutively active mutant of a small GTPase, Cdc42 (Q61L) that causes well characterized changes in cellular morphology [Heo, W.D., and Meyer, T. (2003) Cell 113(3):315–328] was stably expressed, fused to a DD-tag, in NIH 3T3 cells. One population (Panel A) was mock-treated and a second population (Panel B) was treated with 1 μM Shield1 for 24 hr. A third population (Panel C) was treated with 1 μM Shield1 for 24 hr, then washed with media and cultured in the absence of Shield1 for 48 hr. Shield1-treated populations of cells expressing DD-Cdc42 (Q61L) displayed the predicted change in morphology. This change was reversible, as removal of Shield1 resulted in a fibroblast-like morphology indistinguishable from that of mock-treated transduced cells [Banaszynski, L.A., et al. (2006) Cell 126(5):995–1004].

Back

Control of actin stability with the ProteoTuner system

Control of actin stability with the ProteoTuner system

Control of actin stability with the ProteoTuner system. In the absence of Shield1, no DD-AcGFP1 is observed (Panel B) despite the presence of a normal actin filament network (Panel A). In the presence of Shield1, DD-AcGFP1 is stable and present in the actin network (Panel D).

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632172: ProteoTuner Shield System N

632172: ProteoTuner Shield System N
632168 ProteoTuner™ Shield System N (w/ AcGFP1) Each USD $700.00

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 ProteoTuner™ Shield System N (w/ AcGFP1) product License Agreement can be found by clicking here.
39 AcGFP is covered by U.S. Patent No. 7,432,053.
57 This product is covered by U.S. Patent Nos. 8,173,792 and 9,487,787.

Direct manipulation of the presence and absence of a specific protein of interest is a very powerful tool for analyzing protein function. The ProteoTuner Shield System N (w/ AcGFP1) uses a unique method to regulate the amount of protein of interest present in a cell, quickly and directly. It utilizes a ligand-dependent destabilization domain (DD) and its membrane permeable stabilizing ligand, Shield1. The DD is based on a 12 kDa mutant of the FKBP protein, which is expressed as a tag onto the N-terminus of your protein of interest. In the presence of Shield1, the DD-tagged protein is stabilized and will accumulate inside the cell. This ligand-dependent stabilization occurs very quickly, and has been observed as soon as 15–30 minutes after the addition of Shield1. However, in the absence of the protective ligand Shield1, the DD-tagged protein of interest is rapidly degraded. Removing the Shield1 (by splitting the cells into media without Shield1) allows for protein destabilization, causing a fast degradation of the protein of interest. The process of stabilization via Shield1 is reversible, so it is possible to tune the amount of protein of interest present in the cell, by controlling the amount of the Shield1 ligand.

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 Resources

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Dose-dependent stabilization of DD-tagged AcGFP1 fluorescent protein

Dose-dependent stabilization of DD-tagged AcGFP1 fluorescent protein

Dose-dependent stabilization of DD-tagged AcGFP1 fluorescent protein. Cells were transfected with pDD-AcGFP1-PL, treated with the indicated amounts of Shield1, and the amount of stabilized DD-AcGFP1-PL was quantified by Western blot using the Living Colors A.v. Monoclonal Antibody(JL-8) to detect AcGFP1.

Back

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization. A small destabilization domain (DD; blue) is fused to a target protein of interest. The small membrane-permeable ligand Shield1 (red) binds to the DD and protects it from proteasomal degradation. Removal of Shield1 however, causes rapid degradation of the entire fusion protein. The default pathway for the ProteoTuner systems is degradation of the fusion protein unless Shield1 is present.

Back

Predictable and reversible Shield1-dependent regulation of intracellular protein levels

Predictable and reversible Shield1-dependent regulation of intracellular protein levels

Predictable and reversible Shield1-dependent regulation of intracellular protein levels. NIH 3T3 cells stably expressing a DD-tagged yellow fluorescent protein were treated with varying concentrations of Shield1 over the course of one week, and samples of the population were assayed by flow cytometry at the indicated time points [Banaszynski, L. A., et al. (2006) Cell 126(5):995–1004].

Back

Shield1 results in predictable changes in cellular morphology

Shield1 results in predictable changes in cellular morphology

Shield1 results in predictable changes in cellular morphology. A constitutively active mutant of a small GTPase, Cdc42 (Q61L) that causes well characterized changes in cellular morphology [Heo, W.D., and Meyer, T. (2003) Cell 113(3):315–328] was stably expressed, fused to a DD-tag, in NIH 3T3 cells. One population (Panel A) was mock-treated and a second population (Panel B) was treated with 1 μM Shield1 for 24 hr. A third population (Panel C) was treated with 1 μM Shield1 for 24 hr, then washed with media and cultured in the absence of Shield1 for 48 hr. Shield1-treated populations of cells expressing DD-Cdc42 (Q61L) displayed the predicted change in morphology. This change was reversible, as removal of Shield1 resulted in a fibroblast-like morphology indistinguishable from that of mock-treated transduced cells [Banaszynski, L.A., et al. (2006) Cell 126(5):995–1004].

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632168: ProteoTuner Shield System N (w/ AcGFP1)

632168: ProteoTuner Shield System N (w/ AcGFP1)
631072 ProteoTuner™ Shield System C Each USD $700.00

License Statement

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

The ProteoTuner Shield System C utilizes a ligand-dependent destabilization domain (DD-C) and a membrane-permeant stabilizing ligand, Shield1, to quickly and directly regulate the amount of your protein of interest present in a cell or organism. First, your gene of interest is cloned into the pPTunerC Vector and expressed as a fusion with the destabilization domain (DD-C). Then the Shield1 ligand is either added or withheld, depending on your experiment.

In the presence of Shield1, the DD-C-tagged protein is stabilized and accumulates inside the cell. This ligand-dependent stabilization occurs very quickly, and has been observed as soon as 15–30 minutes after the addition of Shield1. In the absence of Shield1, the DD-C-tagged protein of interest is unstable. Consequently, removal of Shield1 allows for active and controllable degradation of the protein of interest. The extent of stabilization via Shield1 can be adjusted, and directly correlates with the amount of the ligand in the medium. Therefore, you can tune the level of your protein of interest present in the cell, by controlling the amount of the Shield1 ligand.

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

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization

Ligand-dependent, targeted and reversible protein stabilization. A small destabilization domain (DD; blue) is fused to a target protein of interest. The small membrane-permeable ligand Shield1 (red) binds to the DD and protects it from proteasomal degradation. Removal of Shield1 however, causes rapid degradation of the entire fusion protein. The default pathway for the ProteoTuner systems is degradation of the fusion protein unless Shield1 is present.

Back

Control of actin stability with the ProteoTuner system

Control of actin stability with the ProteoTuner system

Control of actin stability with the ProteoTuner system. In the absence of Shield1, no DD-AcGFP1 is observed (Panel B) despite the presence of a normal actin filament network (Panel A). In the presence of Shield1, DD-AcGFP1 is stable and present in the actin network (Panel D).

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631072: ProteoTuner Shield System C

631072: ProteoTuner Shield System C

Learn more about our tet, ProteoTuner, and iDimerize inducible systems Inducible systems
Overviews ProteoTuner explained
Selection guides ProteoTuner kit selection guide

Overview

  • Rapid kinetics: protein level changes in minutes allows accurate functional analysis
  • Precise tuning: precise control of protein level by controlling the dose of Shield1
  • Reversible control: "protein on" to "protein off" for convincing gene-function studies
  • What you get: each kit is supplied with a plasmid vector and an aliquot of Shield1.
  • NOTE: Most of the proteins that we tested showed a better destabilization profile when the DD tag was fused to the N-terminus of the protein of interest (Systems N). Specific DD tag mutants for C-terminal tagging are available as well (System C); however they have a slightly reduced destabilization activity in the absence of the Shield1 ligand.

More Information

Applications

  • Protein function in pathways
  • Functional analysis of subunits of a protein complex
  • Functional analysis of essential proteins

Additional product 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.


Control protein stability using a small molecule ligand, Shield1

Control protein stability with Shield1

ProteoTuner systems allow quick, predictable regulation of protein presence or absence in mammalian cells by acting directly on the protein, using a small, cell-permeable synthetic compound. When Shield1 is added to the medium, any fusion protein containing a DD domain can accumulate to detectable levels within 15–20 minutes. Conversely, upon Shield1 removal, the half-time for the protein's degradation can be as short as 30 minutes. This post-translational regulation offers many benefits, from speed and convenience to precise tuning and reversible control.

Technology explained Product selection guide

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Takara Bio USA, Inc. provides kits, reagents, instruments, and services that help researchers explore questions about gene discovery, regulation, and function. As a member of the Takara Bio Group, Takara Bio USA is part of a company that holds a leadership position in the global market and is committed to improving the human condition through biotechnology. Our mission is to develop high-quality innovative tools and services to accelerate discovery.

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Takara Bio USA, Inc. provides kits, reagents, instruments, and services that help researchers explore questions about gene discovery, regulation, and function. As a member of the Takara Bio Group, Takara Bio USA is part of a company that holds a leadership position in the global market and is committed to improving the human condition through biotechnology. Our mission is to develop high-quality innovative tools and services to accelerate discovery.

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  • Cloning
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  • Gene function
  • Protein research
  • Antibodies and ELISA
  • New products
  • Special offers
  • COVID-19 research
  • Viral detection with qPCR
  • SARS-CoV-2 pseudovirus
  • Human ACE2 stable cell line
  • Viral RNA isolation
  • Viral and host sequencing
  • Vaccine development
  • CRISPR screening
  • Drug discovery
  • Immune profiling
  • Publications
  • Next-generation sequencing
  • RNA-seq
  • DNA-seq
  • Single-cell NGS automation
  • Reproductive health
  • Bioinformatics tools
  • Whole genome amplification
  • Immune profiling
  • Diagnostic solutions
  • Reproductive health
  • Real-time PCR
  • Real-time PCR kits
  • Reverse transcription prior to qPCR
  • High-throughput qPCR solutions
  • RNA extraction and analysis for real-time qPCR
  • Stem cell research
  • Media and supplements
  • Stem cells and stem cell-derived cells
  • Single-cell cloning of edited hiPS cells
  • mRNA and cDNA synthesis
  • In vitro transcription
  • cDNA synthesis kits
  • Reverse transcriptases
  • RACE kits
  • Purified cDNA & genomic DNA
  • Purified total RNA and mRNA
  • PCR
  • Most popular polymerases
  • High-yield PCR
  • High-fidelity PCR
  • GC rich PCR
  • PCR master mixes
  • Cloning
  • In-Fusion seamless cloning
  • Competent cells
  • Ligation kits
  • Restriction enzymes
  • Nucleic acid purification
  • Plasmid purification kits
  • Genomic DNA purification kits
  • DNA cleanup kits
  • RNA purification kits
  • Cell-free DNA purification kits
  • Microbiome
  • Gene function
  • Gene editing
  • Viral transduction
  • Fluorescent proteins
  • T-cell transduction and culture
  • Tet-inducible expression systems
  • Transfection reagents
  • Cell biology assays
  • Protein research
  • Purification products
  • Two-hybrid and one-hybrid systems
  • Mass spectrometry reagents
  • Antibodies and ELISA
  • Primary antibodies and ELISAs by research area
  • Fluorescent protein antibodies
  • Special offers
  • Free samples
  • TB Green qPCR sale
  • PrimeSTAR enzyme promo
  • Try BcaBEST DNA Polymerase ver.2.0
  • RNA purification sale
  • Capturem IP and Co-IP sale
  • Baculovirus titration kits early access program
  • NGS bundle and save
  • Free sample: PrimePath Direct Saliva SARS-CoV-2 Detection Kit
  • TALON his-tag purification resin special offer
  • GoStix Plus special offers
  • PCR samples
  • Services & Support
  • Instrument services
  • OEM & custom enzyme manufacturing
  • Stem cell services
  • Gene and cell therapy manufacturing
  • Customer service
  • Sales
  • Shipping & delivery
  • Technical support
  • Feedback
  • Online tools
  • Partnering & Licensing
  • Vector information
  • Instrument services
  • Apollo services
  • ICELL8 services
  • SmartChip services
  • OEM & custom enzyme manufacturing
  • Quality
  • Expertise
  • Stem cell services
  • Clinical-grade stem cell services
  • Research-grade stem cell services
  • Outsourcing stem cell-based disease model development
  • Gene and cell therapy manufacturing
  • Services
  • Facilities
  • Our process
  • Resources
  • Sales
  • Make an appointment with your sales rep
  • Online tools
  • GoStix Plus FAQs
  • Vector information
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  • Vector document finder
  • Learning centers
  • Automation systems
  • Next-generation sequencing
  • cDNA synthesis
  • Real-time PCR
  • Nucleic acid purification
  • PCR
  • Cloning
  • Stem cell research
  • Gene function
  • Protein research
  • Antibodies and ELISA
  • Automation systems
  • SmartChip Real-Time PCR System introduction
  • ICELL8 introduction
  • Next-generation sequencing
  • Technical notes
  • Featured kits
  • Technology and application overviews
  • FAQs and tips
  • DNA-seq protocols
  • Bioinformatics resources
  • Webinars
  • Real-time PCR
  • Overview
  • Reaction size guidelines
  • Guest webinar: extraction-free SARS-CoV-2 detection
  • Guest webinar: developing and validating molecular diagnostic tests
  • Technical notes
  • Nucleic acid purification
  • Nucleic acid extraction webinars
  • Product demonstration videos
  • Product finder
  • Plasmid kit selection guide
  • RNA purification kit finder
  • PCR
  • Citations
  • Selection guides
  • Technical notes
  • FAQ
  • Cloning
  • In-Fusion Cloning general information
  • Primer design and other tools
  • In‑Fusion Cloning tips and FAQs
  • Applications and technical notes
  • Stem cell research
  • Overview
  • Protocols
  • Technical notes
  • Gene function
  • Gene editing
  • Viral transduction
  • T-cell transduction and culture
  • Inducible systems
  • Cell biology assays
  • Protein research
  • Capturem technology
  • Antibody immunoprecipitation
  • His-tag purification
  • Other tag purification
  • Expression systems
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  • Vaccine development
  • Pathogen detection
  • Immunotherapy research
  • Cancer research
  • Alzheimer's disease research
  • Reproductive health technologies
  • Molecular diagnostics
  • Interview: adapting to change with Takara Bio
  • Applications
  • Solutions
  • Partnering
  • Webinar: Speeding up diagnostic development
  • Contact us
  • Vaccine development
  • Characterizing the viral genome and host response
  • Identifying and cloning vaccine targets
  • Expressing and purifying vaccine targets
  • Immunizing mice and optimizing vaccine targets
  • Pathogen detection
  • Sample prep
  • Detection methods
  • Identification and characterization
  • SARS-CoV-2
  • Antibiotic-resistant bacteria
  • Food crop pathogens
  • Waterborne disease outbreaks
  • Viral-induced cancer
  • Immunotherapy research
  • T-cell therapy
  • Antibody therapeutics
  • T-cell receptor profiling
  • TBI initiatives in cancer therapy
  • Cancer research
  • Sample prep from FFPE tissue
  • Sample prep from plasma
  • Cancer biomarker discovery
  • Cancer biomarker quantification
  • Single cancer cell analysis
  • Cancer genomics and epigenomics
  • HLA typing in cancer
  • Gene editing for cancer therapy/drug discovery
  • Alzheimer's disease research
  • Antibody engineering
  • Sample prep from FFPE tissue
  • Single-cell sequencing
  • Reproductive health technologies
  • Preimplantation genetic testing
  • ESM Collection Kit forms
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  • Current events
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  • Gene editing
  • Research news
  • Single-cell analysis
  • Stem cell research
  • Tips and troubleshooting
  • Women in STEM
  • That's Good Support!
  • About our blog
  • That's Good Science!
  • SMART-Seq Pro Biomarker Discovery Contest
  • DNA extraction educational activity
  • That's Good Science Podcast
  • Season one
  • Season two
  • Season three
  • Our brands
  • Takara
  • Clontech
  • Cellartis
  • Events
  • Biomarker discovery events
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