| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HRSP12 |
| Uniprot No | P52758 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-137aa |
| 氨基酸序列 | SSLIRRVISTAKAPGAIGPYSQAVLVDRTIYISGQIGMDPSSGQLVSGGVAEEAKQALKNMGEILKAAGCDFTNVVKTTVLLADINDFNTVNEIYKQYFKSNFPARAAYQVAALPKGSRIEIEAVAIQGPLTTASL |
| 预测分子量 | 41.4kDa |
| 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HRSP12重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Functional characterization of HRSP12 as a novel regulator of NF-κB signaling"
**作者**: Li, X. et al.
**摘要**: 本研究揭示了HRSP12重组蛋白在NF-κB信号通路中的调控作用，证明其通过与IκB激酶复合物相互作用抑制炎症反应，为靶向HRSP12的免疫治疗提供了理论基础。
2. **文献名称**: "Recombinant HRSP12 expression and its role in hepatocellular carcinoma cell apoptosis"
**作者**: Wang, Y. et al.
**摘要**: 通过在大肠杆菌中重组表达HRSP12蛋白，发现其能通过激活线粒体凋亡通路显著抑制肝癌细胞增殖，提示其在肿瘤治疗中的潜在应用价值。
3. **文献名称**: "Structural insights into HRSP12-mediated protein quality control"
**作者**: Zhang, Q. et al.
**摘要**: 利用X射线晶体学解析了HRSP12重组蛋白的三维结构，揭示了其与泛素化蛋白酶体系统的结合机制，阐明了其在错误折叠蛋白降解中的分子基础。
注：以上文献信息为示例性质，实际文献需通过PubMed或Web of Science等平台检索确认。若需具体文章，可进一步提供研究方向(如疾病关联或表达体系)以精准筛选。
**Background of HRSP12 Recombinant Protein**
HRSP12 (Heat Shock Protein 12), also referred to as HSPB8. belongs to the small heat shock protein (sHSP) family, which plays critical roles in cellular stress responses. These proteins act as molecular chaperones, assisting in protein folding, preventing aggregation of denatured proteins, and promoting cell survival under stress conditions such as heat, oxidative stress, or hypoxia. HRSP12 is ubiquitously expressed in mammalian tissues, with notable presence in muscles, neurons, and the heart.
Structurally, HRSP12 contains a conserved α-crystallin domain flanked by variable N- and C-terminal regions, enabling interactions with client proteins and other chaperones. It is implicated in autophagy-lysosomal pathways, particularly through its interaction with BAG3. facilitating the clearance of misfolded proteins—a process vital for maintaining proteostasis. Dysregulation of HRSP12 has been linked to neurodegenerative diseases (e.g., amyotrophic lateral sclerosis), myopathies, and cardiovascular disorders, highlighting its therapeutic potential.
Recombinant HRSP12 is produced using expression systems like *E. coli* or mammalian cells, ensuring high purity and bioactivity for research. Its applications span *in vitro* studies exploring chaperone mechanisms, stress response pathways, and disease models. Additionally, it serves as a tool for drug screening, aiming to modulate its activity in pathologies characterized by protein aggregation.
In summary, HRSP12 recombinant protein is a key reagent for deciphering cellular stress adaptation mechanisms and developing targeted therapies for protein-misfolding diseases.
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