Analytical Data
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基因名
HSP10/EPF/Goat
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简介
The HSP10/EPF protein in collaboration with Hsp60 promotes the correct folding of the input protein and, under stressful conditions in the mitochondrial matrix, prevents misfolding while promoting the refolding and correct assembly of the unfolded polypeptide. The increased expression of HSP10 protein can inhibit the apoptosis of astrocytoma cells and is associated with poor prognosis. HSP10/EPF Protein, Goat/Human/Mouse (His-Avi) is the recombinant human, mouse-derived HSP10/EPF protein, expressed by E. coli , with C-Avi, N-His labeled tag.
- Application
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别名
Cpn10; HSPE1; Hsp10; Chaperonin 10; CPN10; EPF; GROES
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种属
Human; Mouse
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表达系统
E. coli
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标签
N-Avi;N-8*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
A0A8C2NRB8
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表达区间
A2-D102
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蛋白长度
Full Length of Mature Protein
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分子量
13.7 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
HSP10 (Heat Shock Protein 10), EPF (Endoplasmic Reticulum Protein Folding), and goat-derived recombinant proteins have garnered significant attention in biomedical research due to their roles in protein folding, stress response, and potential as therapeutic agents. HSP10, part of the chaperonin family, assists in the proper folding of proteins under stress conditions, which is critical for maintaining cellular homeostasis. EPF contributes to the quality control of protein synthesis, ensuring that misfolded proteins are efficiently processed and degraded. The use of goat as a source for recombinant protein expression offers distinct advantages, such as high yield and the ability to produce complex post-translational modifications, making them suitable for therapeutic applications. Research in this area explores the potential of HSP10 and EPF in enhancing the stability and efficacy of biologics, targeting diseases linked to protein misfolding, such as neurodegenerative disorders. Furthermore, the generation of recombinant proteins in goats provides a cost-effective and scalable approach for producing these essential molecular chaperones, which may lead to advancements in treating various diseases by improving the functional properties of therapeutic proteins. The intersection of molecular biology and biotechnology in this field continues to pave the way for innovative solutions to age-old challenges in medicine.
