Analytical Data
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基因名
HSPBP1
- Application
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别名
FES1; Hsp70 Interacting Protein; Hsp70 Binding Protein,Cytoplasmic Cochaperone 1; Heat shock protein-binding protein 1; Hsp70-interacting protein 1
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种属
Rat
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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 90% as determined by SDS-PAGE.
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蛋白编号
Q6IMX7
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表达区间
Ser198~Asp352
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分子量
21kDa
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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
HSPBP1 (Heat Shock Protein 70 Binding Protein 1) is a crucial co-chaperone in the heat shock protein (HSP) family, primarily known for its role in regulating the activity of HSP70. HSPs play a significant role in protein folding, repair, and cellular stress response, making them vital for maintaining cellular homeostasis. Research indicates that HSPBP1 facilitates the ATPase activity of HSP70, thereby enhancing its chaperone functions and influencing various cellular processes, including protein maturation, degradation, and translocation. Abnormalities in HSPBP1 expression have been linked to several pathophysiological conditions such as cancer, neurodegenerative diseases, and cardiovascular disorders, highlighting its potential as a therapeutic target. The recombinant protein advanced in studies allows for the exploration of HSPBP1's interactions with HSP70 and other client proteins under various stress conditions, aiming to unveil its mechanistic role in protein quality control and cellular resilience. Understanding the functional dynamics of HSPBP1 in cellular stress response may pave the way for novel strategies in treating diseases associated with protein misfolding and aggregation.
