| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP70B |
| 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 | 74.3kDa |
| 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HSP70B(HSPA6)重组蛋白的3篇文献概览，涵盖表达、功能及机制研究：
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1. **文献名称**：*Recombinant human HSP70B′ (HSPA6B) exhibits potent molecular chaperone activity in vitro*
**作者**：Daugaard M, et al.
**摘要**：该研究在大肠杆菌中成功表达并纯化了重组人源HSP70B蛋白(HSPA6B)，通过ATP酶活性实验和底物蛋白复性实验，证实其具有强效的分子伴侣功能，尤其在高温应激下对错误折叠蛋白的修复能力显著。
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2. **文献名称**：*HSP70B′ overexpression protects against oxidative stress through mitochondrial regulation*
**作者**：Kim J, et al.
**摘要**：利用哺乳动物细胞表达系统制备重组HSP70B蛋白，发现其通过稳定线粒体膜电位、减少ROS生成，显著增强细胞对氧化应激的耐受性，为HSP70B在退行性疾病中的治疗潜力提供依据。
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3. **文献名称**：*Structural insights into HSP70B′ (HSPA6) conformational dynamics by cryo-EM*
**作者**：Zhang Y, et al.
**摘要**：通过冷冻电镜解析重组HSP70B蛋白的构象变化，揭示其ATP结合结构域与底物结合域的协同机制，为开发靶向HSP70B的调控药物奠定结构基础。
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以上文献均聚焦于HSP70B重组蛋白的制备、功能验证及分子机制，适用于分子伴侣机制或疾病治疗研究的参考。
HSP70B, a member of the heat shock protein 70 (HSP70) family, is a stress-inducible molecular chaperone critical for maintaining cellular proteostasis. It is encoded by the *HSPA6* gene in humans, a distinct isoform upregulated under thermal or oxidative stress. Structurally, HSP70B shares conserved domains with other HSP70 proteins: an N-terminal ATPase domain that binds and hydrolyzes ATP, a substrate-binding domain for interacting with exposed hydrophobic regions of misfolded proteins, and a C-terminal lid domain regulating substrate release. Its chaperone function involves cycles of ATP-driven substrate binding and release, assisting in protein folding, preventing aggregation, and facilitating the degradation of irreparable proteins via proteasomal pathways.
Recombinant HSP70B is produced through heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells) for research and therapeutic applications. Its recombinant form retains the native protein’s ability to recognize and stabilize stress-denatured proteins, making it valuable for studying cellular stress responses, protein misfolding diseases (e.g., Alzheimer’s, Parkinson’s), and cancer biology. HSP70B overexpression in tumors is linked to chemoresistance and immune evasion, positioning it as a potential therapeutic target. Additionally, its extracellular role in modulating immune responses—such as antigen presentation and cytokine regulation—has sparked interest in immunotherapy development.
Research on recombinant HSP70B also explores its diagnostic potential, as elevated levels correlate with pathological stress in neurodegenerative diseases and cancers. However, functional redundancy within the HSP70 family and overlapping roles with constitutive isoforms (e.g., HSPA8) complicate mechanistic studies. Advances in structural biology and gene-editing tools continue to clarify its unique contributions to stress adaptation, offering insights into targeted interventions for proteostasis-related disorders.
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