| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPB2 |
| Uniprot No | Q16082 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-182aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMSGRSV PHAHPATAEY EFANPSRLGE QRFGEGLLPE EILTPTLYHG YYVRPRAAPA GEGSRAGASE LRLSEGKFQA FLDVSHFTPD EVTVRTVDNL LEVSARHPQR LDRHGFVSRE FCRTYVLPAD VDPWRVRAAL SHDGILNLEA PRGGRHLDTE VNEVYISLLP APPDPEEEEE AAIVEP |
| 预测分子量 | 23 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HSPB2重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Recombinant HSPB2 Enhances Mitochondrial Function and Protects Against Cardiac Ischemia-Reperfusion Injury*
**作者**：Chen L, et al.
**摘要**：该研究利用大肠杆菌系统成功表达并纯化了重组HSPB2蛋白，发现其通过调节线粒体膜电位和减少ROS生成，显著减轻心肌缺血再灌注损伤，揭示了HSPB2在心血管保护中的潜在治疗价值。
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2. **文献名称**：*Structural Characterization of HSPB2 Chaperone Activity Using Recombinant Protein Expression*
**作者**：Smith J, et al.
**摘要**：研究者通过哺乳动物细胞表达系统制备了重组HSPB2.结合X射线晶体学分析其结构，发现HSPB2通过C端结构域与其他小热休克蛋白(如HSPB1)互作，协同维持应激条件下蛋白质的稳定性。
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3. **文献名称**：*HSPB2 Recombinant Protein Attenuates Neurodegeneration in a Parkinson’s Disease Model*
**作者**：Wang Y, et al.
**摘要**：该研究在小鼠帕金森模型中验证了重组HSPB2蛋白的神经保护作用，证明其通过抑制α-突触核蛋白聚集和激活自噬通路，显著延缓多巴胺能神经元退化。
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(注：以上文献为示例性内容，实际文献需通过PubMed或学术数据库检索确认。)
HSPB2 (Heat Shock Protein Family B Member 2), also known as heat shock protein 27kDa-associated protein 2. is a member of the small heat shock protein (sHSP) family. These proteins are characterized by a conserved α-crystallin domain and function as molecular chaperones, assisting in protein folding, preventing aggregation of denatured proteins, and promoting cellular stress resistance. HSPB2 is distinct from its more studied paralog HSPB1 (HSP27) in tissue distribution and structural features. It is predominantly expressed in cardiac and skeletal muscle tissues, where it localizes to mitochondria and cytoplasm, suggesting roles in energy metabolism and stress response.
Recombinant HSPB2 protein is produced using genetic engineering techniques, typically expressed in bacterial or mammalian systems to ensure proper folding and post-translational modifications. Its production enables in vitro studies to dissect molecular mechanisms, such as interactions with client proteins (e.g., misfolded proteins or components of the ubiquitin-proteasome system) and regulatory pathways involving phosphorylation. Research highlights its involvement in mitigating oxidative stress, modulating autophagy, and maintaining mitochondrial integrity. Dysregulation of HSPB2 has been implicated in neuromuscular disorders, cardiomyopathies, and neurodegenerative diseases like Alzheimer’s, making it a potential therapeutic target.
Current studies focus on its chaperone activity, oligomerization dynamics, and crosstalk with other stress-response pathways. Recombinant HSPB2 also serves as a tool for antibody development and biomarker discovery. Despite progress, questions remain about its precise physiological roles, tissue-specific regulation, and therapeutic applicability, driving ongoing investigations into its structure-function relationships and disease associations.
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