Analytical Data
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基因名
clpB
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简介
ClpB protein is a key component in the stress-induced multichaperone system, which cooperates with DnaK, DnaJ and GrpE to promote cell recovery from heat-induced injury. Upstream of DnaK, ClpB processes protein aggregates and upon binding stimulates their ATPase activity. clpB Protein, E.coli (K476C) is the recombinant E. coli-derived clpB protein, expressed by E. coli , with tag free.
- Application
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别名
clpB; Chaperone protein ClpB
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种属
E.coli
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P63286
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表达区间
M1-Q857, K476C
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蛋白长度
Full Length
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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
ClpB is a heat-shock protein belonging to the AAA+ ATPase family, crucial for protein quality control in cells. Its primary function is to facilitate the refolding of aggregated proteins, thereby maintaining cellular protein homeostasis, especially under stress conditions such as heat shock or oxidative stress. ClpB operates in concert with other molecular chaperones, such as GroEL and DnaK, forming a sophisticated cellular machinery that prevents protein misfolding and aggregation. Research on recombinant ClpB has gained significant interest due to its potential applications in biotechnology and medicine. It has been studied for its role in enhancing protein solubility, aiding in the refolding of therapeutic proteins, and improving yields in recombinant protein production. Furthermore, understanding ClpB's structure and function could provide insights into the molecular mechanisms of protein aggregation diseases, such as Alzheimer's and Parkinson's. By manipulating ClpB through genetic engineering or chemical modifications, scientists aim to develop novel strategies to combat these diseases and improve the biopharmaceutical production process. As a result, ClpB serves as a model system for investigating protein dynamics and chaperone interactions, making its study vital for advancing both basic and applied biological research.
