Analytical Data
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基因名
HSPA13
- Application
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别名
Microsomal stress-70 protein ATPase core;Stress-70 protein chaperone microsome-associated 60KDA protein
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P48723
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表达区间
23-471aa
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分子量
76.6 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
HSPA13, also known as heat shock protein family A member 13, is a member of the HSP70 chaperone family that plays a critical role in cellular stress responses, protein folding, and the maintenance of cellular homeostasis. It is implicated in a variety of cellular processes, including signal transduction, apoptosis, and the regulation of protein synthesis. The research on HSPA13 recombinant protein has gained attention due to its potential therapeutic applications in various diseases, such as neurodegenerative disorders and cancers. The ability of HSPA13 to assist in the proper folding of proteins and to protect cells from stress-induced damage positions it as a key player in understanding the molecular mechanisms of these diseases. Furthermore, recombinant HSPA13 protein can be utilized to study protein-protein interactions and to investigate its specific functions within various cellular contexts. The development of tools to produce and purify HSPA13 in a laboratory setting has opened new avenues for exploring its role in disease models and has the potential to contribute to the development of novel therapeutic strategies. Understanding HSPA13's structure and function at a molecular level could provide insights into its biological significance and could pave the way for the design of small molecules or biologics that modulate its activity, enhancing cellular resilience in disease states. Overall, the study of HSPA13 recombinant protein represents a promising frontier in biomedical research, with the potential to uncover novel insights into protein homeostasis and its implications for human health.












