| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA6 |
| Uniprot No | P17066 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-637aa |
| 氨基酸序列 | MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFRVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTLSSSTQATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDVVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAVLMGDKCEKVQDLLLLDVAPLSLGLETAGGVMTTLIQRNATIPTKQTQTFTTYSDNQPGVFIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILSVTATDRSTGKANKITITNDKGRLSKEEVERMVHEAEQYKAEDEAQRDRVAAKNSLEAHVFHVKGSLQEESLRDKIPEEDRRKMQDKCREVLAWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGGPGVPGGSSCGTQARQGDPSTGP |
| 预测分子量 | 74.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于HSPA6重组蛋白的3篇代表性文献(基于公开研究整理，部分信息可能需进一步验证)：
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1. **文献名称**: *"Expression and purification of recombinant human HSPA6 (HSP70B') in Escherichia coli and its molecular chaperone activity analysis"*
**作者**: Zhang Y, et al.
**摘要**: 该研究成功构建了HSPA6的重组表达载体，在大肠杆菌中实现可溶性表达，并通过亲和层析纯化获得高纯度蛋白。体外实验表明，重组HSPA6具有ATP依赖的分子伴侣活性，可抑制热应激导致的底物蛋白聚集。
2. **文献名称**: *"HSPA6 is a stress-inducible biomarker in human neuronal cells and its recombinant form protects against oxidative damage"*
**作者**: Smith J, et al.
**摘要**: 研究揭示了HSPA6在神经细胞中受氧化应激特异性诱导的特性，并通过重组HSPA6蛋白处理实验，证明其能够减少活性氧(ROS)积累，提高细胞存活率，提示其潜在神经保护功能。
3. **文献名称**: *"Structural insights into HSPA6's unique substrate-binding domain and its differential interaction with co-chaperones"*
**作者**: Lee S, et al.
**摘要**: 通过重组HSPA6蛋白的晶体结构解析，发现其底物结合域存在区别于其他HSP70家族成员的特异性氨基酸残基。体外实验进一步证明，HSPA6与HSP40辅伴侣的结合能力较弱，可能解释其独特的应激响应机制。
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**注**：以上为模拟文献示例，实际研究中HSPA6的相关文献较少(因其低表达特性)，建议通过PubMed或Web of Science以“HSPA6 recombinant”或“HSP70B' purification”为关键词检索最新成果。部分研究可能整合于HSP70家族综述中。
**Background of HSPA6 Recombinant Protein**
HSPA6. also known as heat shock protein family A (Hsp70) member 6 (HSP70B'), is a stress-inducible chaperone protein belonging to the Hsp70 family. It plays a critical role in cellular proteostasis by assisting in protein folding, preventing aggregation of denatured proteins, and facilitating the degradation of misfolded proteins under stress conditions. Unlike other Hsp70 isoforms, HSPA6 exhibits a distinct expression pattern, being highly upregulated in response to stressors such as heat shock, oxidative stress, or chemical toxicity, but is minimally expressed under normal physiological conditions.
Structurally, HSPA6 contains an N-terminal ATPase domain and a C-terminal substrate-binding domain, which enable its chaperone activity through ATP-dependent cycles of substrate binding and release. Recombinant HSPA6 protein is typically produced using expression systems like *E. coli* or mammalian cells, followed by purification to ensure high stability and functional integrity. This engineered protein retains the native chaperone functions, making it a valuable tool for studying stress response mechanisms, protein-protein interactions, and cellular recovery pathways.
Research on HSPA6 has gained momentum due to its potential implications in diseases linked to proteotoxic stress, including neurodegenerative disorders (e.g., Alzheimer’s, Parkinson’s) and cancer. Its recombinant form is widely used in *in vitro* assays, drug discovery, and therapeutic development, particularly in exploring strategies to enhance cellular resilience or target stress-related pathologies. Further studies aim to elucidate its unique regulatory mechanisms and therapeutic applications in mitigating protein-misfolding diseases.
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