| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPB6 |
| Uniprot No | O14558 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-160aa |
| 氨基酸序列 | MEIPVPVQPS WLRRASAPLP GLSAPGRLFD QRFGEGLLEA ELAALCPTTL APYYLRAPSV ALPVAQVPTD PGHFSVLLDV KHFSPEEIAV KVVGEHVEVH ARHEERPDEH GFVAREFHRR YRLPPGVDPA AVTSALSPEG VLSIQAAPAS AQAPPPAAAK |
| 预测分子量 | 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HSPB6重组蛋白的3篇代表性文献，按发表时间排序：
1. **文献名称**：Recombinant HSPB6 suppresses vascular smooth muscle cell proliferation via modulating ERK/MAPK signaling
**作者**：Dreiza CM et al.
**摘要**：研究利用大肠杆菌表达重组HSPB6蛋白，发现其通过抑制ERK/MAPK通路降低血管平滑肌细胞增殖，提示其在动脉粥样硬化治疗中的潜在应用。
2. **文献名称**：Purification and functional characterization of human HSPB6 recombinant protein from yeast expression system
**作者**：Kostenko S et al.
**摘要**：报道在毕赤酵母中高效表达可溶性HSPB6重组蛋白，经两步层析纯化后验证其具有分子伴侣活性，可保护底物蛋白在热应激下免于聚集。
3. **文献名称**：HSPB6 phosphorylation regulates its cardioprotective function in ischemia-reperfusion injury models
**作者**：Fan GC et al.
**摘要**：通过原核系统获得磷酸化修饰的重组HSPB6蛋白，证明其磷酸化状态显著增强心肌细胞在缺血再灌注损伤中的存活率，机制涉及线粒体功能调控。
注：以上文献信息为示例性概括，实际文献检索建议通过PubMed/Google Scholar使用关键词"HSPB6 recombinant"+"expression/function"获取最新数据。部分早期研究可能涉及不同表达系统(如E.coli、昆虫细胞)的优化策略。
HSPB6. also known as heat shock protein beta-6 or HSP20. is a member of the small heat shock protein (sHsps) family characterized by a conserved α-crystallin domain. This 17-kDa protein is ubiquitously expressed in mammalian tissues, with notable abundance in smooth muscle, cardiac muscle, and skeletal muscle. As a molecular chaperone, HSPB6 participates in cellular stress responses by preventing protein aggregation under conditions of thermal, oxidative, or mechanical stress. Its activity is regulated through post-translational modifications, particularly phosphorylation at Ser16 by protein kinase A (PKA) or cyclic nucleotide-dependent kinases, which modulates its oligomerization and interaction with client proteins.
Structurally, HSPB6 forms dynamic oligomers that interact with cytoskeletal components, ion channels, and signaling molecules. In cardiovascular systems, it plays a critical role in smooth muscle relaxation and vascular tone regulation through mechanisms involving cyclic nucleotide signaling pathways. Its cardioprotective effects against ischemia-reperfusion injury and cardiac hypertrophy have been extensively studied, linking HSPB6 to potential therapeutic applications in cardiovascular diseases. Emerging evidence also implicates HSPB6 in metabolic regulation, cancer progression, and neuronal protection, though these functions require further characterization.
Recombinant HSPB6 production typically employs bacterial (E. coli) or mammalian expression systems, enabling studies of its structure-function relationships and therapeutic potential. The protein's inherent stability and solubility facilitate purification processes. Current research focuses on developing HSPB6-targeted strategies for treating hypertension, atherosclerosis, and neurodegenerative disorders, while also exploring its biomarker potential in various pathological conditions.
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