Analytical Data
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基因名
arsR
- Application
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别名
arsR；Transcriptional regulatory Protein ArsR
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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
P37309
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表达区间
1-117aa
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氨基酸序列
MSFLLPIQLFKILADETRLGIVLLLSELGELCVCDLCTALDQSQPKISRHLALLRESGLLLDRKQGKWVHYRLSPHIPAWAAKIIDEAWRCEQEKVQAIVRNLARQNCSGDSKNICS
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分子量
19.0 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
Related Products
Protein Description
ArsR is a regulatory protein that plays a crucial role in the response to arsenic and antimony stress in various microorganisms. As a member of the ArsR/SmtB family of transcriptional regulators, ArsR binds to metal ions, particularly arsenic, leading to conformational changes that modulate gene expression related to metal detoxification and homeostasis. The study of recombinant ArsR proteins has gained significance due to their potential applications in bioremediation and environmental biotechnology. Understanding the mechanisms by which ArsR senses and responds to toxic metals aids in elucidating microbial adaptation strategies in contaminated environments. Moreover, the structural characterization of recombinant ArsR provides insights into metal binding sites and the regulatory pathways involved in arsenic resistance. This research can also contribute to the development of biosensors for detecting arsenic levels in environmental samples. Overall, the investigation of ArsR not only deepens our comprehension of microbial metal metabolism but also holds promise for addressing global challenges related to arsenic contamination and public health.
