Analytical Data
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基因名
HSP10/EPF
- Application
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别名
HSPE1; CPN10; EPF; GROES; Chaperonin 10; Early Pregnancy Factor; 10 kDa heat shock protein, mitochondrial
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种属
Mouse
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
q64433
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表达区间
Ala2~Asp102
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分子量
12kDa
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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
HSP10 (Heat Shock Protein 10) and EPF (Extracellular Protein Factor) are two important proteins that have garnered significant research interest due to their roles in cellular stress responses and protein folding. HSP10 is a mitochondrial chaperonin that assists in the proper folding of newly synthesized polypeptides, while EPF is known to provide protective functions in various cellular processes, including immunity and adaptation to environmental stressors. The study of HSP10/EPF recombinant proteins has gained momentum, particularly in the context of understanding their molecular mechanisms and potential therapeutic applications. Recent advancements in recombinant DNA technology have enabled researchers to produce these proteins in higher quantities and with increased purity, facilitating in vitro and in vivo studies. Investigating the interactions between HSP10 and EPF may reveal new insights into their complementary roles in protein maturation and stress response pathways. Additionally, the development of recombinant forms of these proteins could lead to novel therapeutic strategies for diseases associated with protein misfolding and aggregation, such as neurodegenerative disorders. Overall, the exploration of HSP10/EPF recombinant proteins holds promise not only for fundamental biological research but also for the advancement of clinical applications aimed at enhancing cellular resilience and function.
