Analytical Data
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基因名
tetR
- Application
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别名
tetR;Phenylalanine-4-hydroxylase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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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
1-207aa
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氨基酸序列
MSRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFCPLEGESWQDFLRNNAKSFRCALLSHRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHFTLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLFGLELIICGLEKQLKCESGS
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分子量
23.4 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
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.












