| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP70 |
| Uniprot No | P0DMV8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-641aa |
| 氨基酸序列 | MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D |
| 预测分子量 | 70 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. |
1. **文献名称**: "Recombinant HSP70 protein as a potent vaccine adjuvant for cancer immunotherapy"
**作者**: Wang Y, et al.
**摘要**: 研究验证了重组HSP70蛋白通过激活树突状细胞和增强抗原呈递，显著提升抗肿瘤T细胞免疫应答，为癌症疫苗开发提供理论基础。
2. **文献名称**: "Expression and purification of functional human HSP70 in Escherichia coli for structural studies"
**作者**: Smith J, et al.
**摘要**: 开发了一种高效的大肠杆菌表达系统，成功获得具有ATP酶活性的重组人源HSP70蛋白，并解析其与底物结合的构象变化机制。
3. **文献名称**: "HSP70 chaperone function in neurodegenerative disease: Amyloid-β suppression via recombinant HSP70 delivery"
**作者**: Lee S, et al.
**摘要**: 体外实验表明，重组HSP70蛋白通过抑制β淀粉样蛋白聚集并促进其降解，减缓阿尔茨海默病模型中神经元损伤。
4. **文献名称**: "Heat shock protein 70 enhances bacterial antigen cross-presentation in macrophages"
**作者**: Tanaka K, et al.
**摘要**: 重组HSP70蛋白通过结合病原体抗原，增强巨噬细胞对胞内细菌的吞噬及抗原交叉呈递能力，提示其在抗感染免疫中的应用潜力。
(注：上述文献信息为示例性内容，实际需根据具体论文调整。)
HSP70 (Heat Shock Protein 70) is a highly conserved family of molecular chaperones crucial for maintaining cellular homeostasis under stress conditions. These 70-kDa proteins are ubiquitously expressed across organisms and play pivotal roles in protein folding, preventing aggregation of misfolded proteins, facilitating intracellular trafficking, and promoting degradation of irreparable proteins via proteasomal pathways. Their expression is upregulated during cellular stress, such as heat shock, oxidative damage, or nutrient deprivation, earning them the "heat shock protein" designation.
Recombinant HSP70 proteins are engineered using genetic cloning techniques, often expressed in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems to ensure high purity and consistent activity. Structural studies reveal two main domains: an N-terminal ATPase domain that binds and hydrolyzes ATP, and a C-terminal substrate-binding domain that interacts with exposed hydrophobic regions of client proteins. This ATP-dependent cycle enables HSP70 to stabilize nascent polypeptides, refold denatured proteins, or target damaged ones for degradation.
In research, recombinant HSP70 is widely used to study stress response mechanisms, protein-protein interactions, and chaperone-mediated autophagy. Its involvement in immune modulation—acting as a danger signal to activate dendritic cells and enhance antigen presentation—has spurred interest in vaccine development and cancer immunotherapy. Additionally, HSP70 dysregulation is linked to neurodegenerative diseases (e.g., Alzheimer’s, Parkinson’s) and cancer, making it a therapeutic target. Recombinant variants, including mutants with altered ATPase activity or tagged versions (e.g., His-tag, fluorescent tags), enable precise mechanistic studies. Current challenges include optimizing stability and delivery methods for clinical applications while addressing its dual roles in promoting cell survival or apoptosis, depending on context.
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