Analytical Data
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Gene name
tetR
- Application
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Alternative Names
tetR；Phenylalanine-4-hydroxylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04483
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Expression Region
1-207aa
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AA Sequence
MSRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFCPLEGESWQDFLRNNAKSFRCALLSHRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHFTLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLFGLELIICGLEKQLKCESGS
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Molecular Weight
23.4 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
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Protein Description
The TetR protein, a key member of the TetR family of transcriptional regulators, plays a crucial role in bacterial response to tetracycline antibiotics and is involved in the regulation of various operons. Initially discovered in Escherichia coli, TetR functions by binding to specific DNA sequences, thereby repressing the expression of genes responsible for antibiotic resistance. This protein exhibits a remarkable ability to sense environmental signals, such as the presence of tetracycline, leading to a conformational change that reduces its affinity for DNA and subsequently activates gene expression. The study of TetR has garnered significant interest not only due to its implications in antibiotic resistance but also owing to its potential applications in synthetic biology. By engineering TetR and its variants, researchers aim to develop tools for controlled gene expression in various organisms. Furthermore, understanding the molecular mechanisms underlying TetR's function can provide insights into the broader complexities of bacterial adaptation and survival. Recent advances in structural biology and high-throughput screening techniques have facilitated the exploration of TetR mutants with altered regulatory properties, unlocking possibilities for innovative applications in therapeutic strategies and biotechnology. As antibiotic resistance remains a pressing global challenge, continued research on TetR and related regulators is essential to devising novel approaches for combating resistant strains and ensuring effective treatment options.
