Analytical Data
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Gene name
TetR
- Application
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21337
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Expression Region
1-211aa
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Molecular Weight
27.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
TetR, or Tetracycline repressor, is a well-known transcriptional regulator originally identified in bacteria as a key player in the tetracycline antibiotic resistance mechanism. This protein functions by binding to specific DNA sequences, thereby inhibiting the transcription of genes responsible for antibiotic uptake and resistance. Its ability to bind to tetracycline and related compounds allows it to modulate gene expression in response to external signals. The study of TetR and its variants has gained significant attention due to their potential applications in synthetic biology and gene regulation. Researchers have explored its use in developing inducible expression systems, which can precisely control gene expression in various organisms, facilitating advancements in biotechnology, gene therapy, and metabolic engineering. Additionally, the structural and functional characterization of TetR has provided insights into its mechanisms of action, leading to the design of novel therapeutics and biosensors. Understanding the intricacies of TetR interactions, both with DNA and small-molecule ligands, is critical for harnessing its capabilities and improving its functionality in research and therapeutic contexts. As a model system, TetR continues to serve as a fundamental tool for elucidating gene regulatory networks and advancing our understanding of cellular function in response to environmental changes.
