| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPB1 |
| Uniprot No | P04792 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-205aa |
| 氨基酸序列 | MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK |
| 分子量 | 22.7 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人HSPB1蛋白的模拟参考文献示例(基于领域内相关研究的合理概括，非真实文献)：
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1. **文献名称**：*Structural and functional analysis of recombinant human HSPB1*
**作者**：Mymrikov EV, et al.
**摘要**：该研究利用大肠杆菌表达系统成功纯化了重组人HSPB1蛋白，并通过X射线晶体学解析了其寡聚体结构，揭示了其分子伴侣活性依赖于温度依赖性构象变化。
2. **文献名称**：*Recombinant HSPB1 suppresses apoptosis in cancer cells under oxidative stress*
**作者**：Garrido C, et al.
**摘要**：研究通过体外实验证明，重组HSPB1蛋白通过抑制线粒体途径的Caspase激活，降低活性氧(ROS)水平，从而增强肿瘤细胞在氧化应激条件下的存活能力。
3. **文献名称**：*HSPB1 phosphorylation modulates its chaperone activity in neurodegenerative models*
**作者**：Arrigo AP, et al.
**摘要**：利用重组磷酸化突变体HSPB1蛋白，发现其Ser15/Ser82位点的磷酸化调控与α-突触核蛋白聚集的相互作用，可能影响帕金森病模型的神经保护作用。
4. **文献名称**：*High-yield production of recombinant HSPB1 in mammalian cells and its role in thermotolerance*
**作者**：Vos MJ, et al.
**摘要**：通过在HEK293细胞中重组表达HSPB1.实现高产量蛋白制备，并验证其通过稳定细胞骨架蛋白增强细胞耐热性的功能。
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**注**：以上文献内容为示例性概括，具体研究需参考真实发表的论文。如需实际文献，建议通过PubMed或Google Scholar搜索关键词“recombinant HSPB1/HSP27”获取。
Heat shock protein B1 (HSPB1), also known as HSP27. is a member of the small heat shock protein (sHSP) family characterized by a conserved α-crystallin domain. It functions as a molecular chaperone, preventing aggregation of misfolded proteins under stress conditions, such as heat shock, oxidative stress, or chemical toxicity. HSPB1 plays critical roles in maintaining cytoskeletal stability, regulating apoptosis, and modulating cellular responses to inflammation and proteotoxic damage. Its activity is dynamically regulated by phosphorylation, which alters oligomerization and client protein interactions.
Recombinant human HSPB1 is produced using expression systems like *E. coli* or mammalian cells, enabling studies of its structure-function relationships and therapeutic potential. Purification typically involves affinity chromatography and refolding steps to ensure proper conformational integrity. Recombinant HSPB1 is widely used in vitro and in vivo to investigate its protective mechanisms in diseases linked to protein misfolding, including neurodegenerative disorders (e.g., Alzheimer’s, ALS), cancer, and cardiovascular diseases. Mutations in HSPB1 are associated with Charcot-Marie-Tooth neuropathy and cataracts, making recombinant variants valuable for dissecting pathogenic mechanisms.
Research on recombinant HSPB1 also explores its dual role in cancer—promoting tumor survival under stress yet potentially enhancing chemoresistance. Its extracellular presence in certain cancers has spurred interest in diagnostic or prognostic biomarker development. Additionally, HSPB1-based therapeutic strategies, including peptide mimetics or gene therapy, are being investigated to modulate cellular stress responses in age-related and protein-aggregation diseases.
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