ProteoTuner expression systems in lentiviral and retroviral formats
Lentiviral and retroviral ProteoTuner systems make it possible to investigate the function of a specific protein of interest directly—by rapidly changing the abundance of the protein itself. These systems utilize a ligand-dependent destabilization domain (DD), and the ligand Shield1 to reversibly stabilize and destabilize a DD-tagged protein of interest in a predictable and dose-dependent manner. Your protein of interest is fused to a DD tag and rapidly stabilized by adding the Shield1 ligand to the culture medium. Plasmid formats are also available.
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 show a better destabilization profile when the DD tag is fused to the N-terminus of the protein of interest (N Systems). Specific DD tag mutants for C-terminal tagging are available as well (C System); however, they have a slightly reduced destabilization activity in the absence of the Shield1 ligand.
- For retrovirus production, use in combination with our Retro-X Universal Packaging System.
- For lentivirus production, use in combination with our Lenti-X Packaging Single Shots.
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 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.
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