Analytical Data
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基因名
TetR
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简介
TetR protein acts as a repressor of the tetracycline resistance element and utilizes the helix-turn-helix structure of its N-terminal region for DNA binding. Tetracycline binding induces a conformational change in TetR that reduces its affinity to the tetA promoter operator site. TetR Protein, E.coli (His) is the recombinant E.coli-derived TetR, expressed by E. coli, with N-6*His labeled tag.
- Application
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别名
tetR; Tetracycline repressor protein class B from transposon Tn10
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种属
E.coli
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表达系统
E. coli
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标签
N-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P04483
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表达区间
M1-S207
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氨基酸序列
MSRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFCPLEGESWQDFLRNNAKSFRCALLSHRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHFTLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLFGLELIICGLEKQLKCESGS
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蛋白长度
Full Length
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分子量
24.0 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
TetR (Tetracycline repressor) is a well-studied bacterial transcriptional regulator that plays a crucial role in antibiotic resistance mechanisms, particularly related to tetracycline antibiotics. Originating from *Escherichia coli*, TetR functions by binding to specific DNA sequences and inhibiting the transcription of target genes involved in tetracycline transport and resistance. Research on TetR has garnered significant interest due to its potential applications in genetic engineering, synthetic biology, and biotechnological advancements. The ability to manipulate TetR for controlled gene expression has led to the development of advanced gene regulation systems, such as tetracycline-controlled transcriptional activation or repression systems. These systems allow precise modulation of gene expression in response to tetracycline or its derivatives, offering valuable tools for studying gene function and developing therapeutic strategies. Additionally, understanding the structural and mechanistic features of TetR can provide insights into the evolution of antibiotic resistance in bacteria and create avenues for designing new antibiotics or enhancing existing treatments. Overall, the study of TetR and its recombinant protein forms remains a pivotal area of research with implications spanning from fundamental microbiology to applied biomedical sciences.
