| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPB3 |
| Uniprot No | Q12988 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-150aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAKIILRHLIEIPVRYQEEFEARGLEDCRL DHALYALPGPTIVDLRKTRAAQSPPVDSAAETPPREGKSHFQILLDVVQF LPEDIIIQTFEGWLLIKAQHGTRMDEHGFISRSFTRQYKLPDGVEIKDLS AVLCHDGILVVEVKDPVGTK |
| 预测分子量 | 19 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HSPB3重组蛋白的假设性参考文献示例(注：以下内容为模拟生成，非真实存在的文献)：
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1. **标题**: *Recombinant HSPB3 Expression and Its Role in Muscle Atrophy*
**作者**: Smith A, et al.
**摘要**: 研究利用大肠杆菌系统成功表达并纯化HSPB3重组蛋白，发现其在体外抑制肌原纤维蛋白聚集，提示其可能通过调节蛋白质稳态延缓肌肉萎缩。
2. **标题**: *Structural Characterization of HSPB3 and Implications for Charcot-Marie-Tooth Disease*
**作者**: Chen L, et al.
**摘要**: 通过重组HSPB3的晶体结构分析，揭示其N端结构域突变与Charcot-Marie-Tooth病的关系，为疾病机制提供分子层面解释。
3. **标题**: *HSPB3 Recombinant Protein Attenuates Oxidative Stress in Cardiomyocytes*
**作者**: Wang Y, et al.
**摘要**: 在心肌细胞模型中，外源性添加重组HSPB3蛋白显著减少氧化应激损伤，表明其在心肌保护中的潜在治疗价值。
4. **标题**: *Comparative Analysis of HSPB3 and HSPB1 Chaperone Activity Using Recombinant Proteins*
**作者**: Gonzalez R, et al.
**摘要**: 比较重组HSPB3与HSPB1的分子伴侣功能，发现HSPB3对特定底物(如α-突触核蛋白)具有更高的结合亲和力，提示功能特异性。
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注：以上文献为模拟生成，实际研究中请通过PubMed、Google Scholar等平台检索真实发表的论文。
**Background of HSPB3 Recombinant Protein**
HSPB3 (Heat Shock Protein Family B Member 3), also known as HSPL27 or Hsp27-3. 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 under stress, and maintaining cellular homeostasis. HSPB3 is less studied compared to other sHSPs like HSPB1 (Hsp27) or HSPB5 (αB-crystallin), but emerging research highlights its unique roles in neuromuscular and neuronal systems.
Expressed predominantly in skeletal and cardiac muscles, HSPB3 is implicated in maintaining cytoskeletal integrity and protecting cells from stress-induced damage. Mutations or dysregulation of HSPB3 have been linked to neuromuscular disorders, including distal hereditary motor neuropathy (dHMN) and Charcot-Marie-Tooth disease (CMT). For instance, specific HSPB3 variants (e.g., R7S) disrupt its chaperone activity or interaction with other proteins, contributing to axonal degeneration and muscle atrophy.
Recombinant HSPB3 protein is produced using expression systems like *E. coli* or mammalian cells, enabling studies of its structure-function relationships, interactome, and pathological mechanisms. Its recombinant form retains the ability to form oligomers and bind client proteins, making it valuable for *in vitro* assays, drug screening, or exploring therapeutic strategies for HSPB3-related diseases. Additionally, recombinant HSPB3 aids in elucidating its role in cellular stress responses, autophagy, and cytoskeletal dynamics, offering insights into broader sHSP biology.
Despite its lower abundance, HSPB3’s tissue-specific expression and disease associations underscore its importance in neuromuscular health, driving interest in recombinant tools to decode its mechanisms and therapeutic potential.
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