Analytical Data
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基因名
HSP70/HSPA1A
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简介
The HSP70/HSPA1A protein is an important molecular chaperone that protects proteome integrity by counteracting stress, aiding protein folding, activating misfolded proteolysis, and regulating protein complex dynamics. In protein quality control systems, it ensures accurate protein folding, controls substrate targeting for degradation through the ATP cycle, and interacts with co-chaperones such as HSP40, BAG1/2/3, HOPX, and STUB1. HSP70/HSPA1A Protein, Human (E110D, His) is the recombinant human-derived HSP70/HSPA1A protein, expressed by E. coli , with N-His labeled tag and E110D mutation.
- Application
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别名
HSP70-1; HSPA1A; HSP72 ; HSPA1; HSX70
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种属
Human
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表达系统
E. coli
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标签
N-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0DMV8-1
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表达区间
A2-D641, E110D
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蛋白长度
Full Length of Isoform-1 Mature Protein
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分子量
72.2 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
HSP70, specifically the HSPA1A isoform, is a heat shock protein that plays a critical role in cellular stress responses, protein folding, and protection against apoptosis. It functions as a molecular chaperone, facilitating the proper folding of nascent polypeptides and the refolding of misfolded proteins, thereby maintaining cellular homeostasis. The expression of HSPA1A is induced under stressful conditions, including heat shock, oxidative stress, and exposure to toxins, highlighting its essential role in protecting cells from damage. Research into HSP70/HSPA1A recombinant proteins has gained significant attention due to their potential therapeutic applications in various diseases, including cancer and neurodegenerative disorders. These studies focus on understanding the mechanistic pathways mediated by HSPA1A and exploring its role in modulating immune responses, cellular signaling, and apoptosis. By generating recombinant HSPA1A, researchers aim to investigate its efficacy as a vaccine adjuvant, diagnostic tool, and therapeutic agent. The ability to produce HSPA1A in a recombinant form allows for detailed biochemical studies and the development of potential interventions to enhance its protective functions in disease contexts. Furthermore, understanding the implications of HSP70/HSPA1A in cellular health and disease could lead to novel strategies for treating conditions associated with protein misfolding and aggregation. Overall, the study of HSP70/HSPA1A recombinant proteins is pivotal in advancing our knowledge of cell biology and developing innovative therapeutic approaches.
