| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPb8 |
| Uniprot No | Q9UJY1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-196aa |
| 氨基酸序列 | MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPD WALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCV NVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVD PVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT |
| 预测分子量 | 50kDa |
| 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. |
1. **"HSPB8 promotes the clearance of ubiquitinated protein aggregates by stabilizing BAG3"**
*作者: Carra S, et al.*
摘要：研究揭示了HSPB8通过与BAG3蛋白结合，增强自噬途径对泛素化蛋白聚集体的清除能力，为神经退行性疾病的治疗提供新思路。
2. **"HSPB8 modulates protein aggregation in cellular models of spinocerebellar ataxia"**
*作者: Rusmini P, et al.*
摘要：通过重组HSPB8蛋白实验，发现其能减少脊髓小脑共济失调模型中突变ataxin-3蛋白的聚集，并协同分子伴侣系统增强错误蛋白的降解。
3. **"Characterization of recombinant human HSPB8 in chaperone-assisted protein folding"**
*作者: Crippa V, et al.*
摘要：报道了重组人HSPB8蛋白的表达与纯化方法，并证明其与HSPB1协同作用，在体外抑制热应激导致的客户蛋白聚集，提升细胞存活率。
4. **"HSPB8 overexpression protects against Aβ toxicity in Alzheimer's disease models"**
*作者: Yu H, et al.*
摘要：利用重组HSPB8蛋白，验证其在阿尔茨海默病细胞模型中通过激活自噬和减少β-淀粉样蛋白毒性，发挥神经保护作用的分子机制。
HSPB8. also known as heat shock protein beta-8 or Hsp22. is a member of the small heat shock protein (sHSP) family characterized by its molecular chaperone activity. These proteins play critical roles in maintaining cellular homeostasis, particularly under stress conditions, by preventing protein misfolding and aggregation. HSPB8 is distinguished by its α-crystallin domain, a conserved structural feature that facilitates interactions with partially unfolded client proteins, promoting their refolding or targeting them for degradation via autophagy. Unlike some sHSPs, HSPB8 exhibits selective substrate specificity and is implicated in regulating processes such as apoptosis, autophagy, and cytoskeletal organization.
Recombinant HSPB8 refers to the protein produced through genetic engineering in heterologous expression systems (e.g., *E. coli*, mammalian cells). Its recombinant production enables precise study of its structure-function relationships, post-translational modifications, and interactions with co-chaperones like BAG3 (BCL2-associated athanogene 3), which is essential for its role in chaperone-assisted selective autophagy (CASA). This pathway is vital for clearing toxic protein aggregates linked to neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), Alzheimer’s, and Huntington’s disease.
Research on recombinant HSPB8 has accelerated due to its therapeutic potential. Studies suggest it may mitigate proteinopathy-driven pathologies by enhancing aggregate clearance or modulating stress signaling pathways. Additionally, HSPB8 overexpression has been linked to cancer progression and chemoresistance, making it a dual-interest target in oncology. The availability of recombinant HSPB8 allows for *in vitro* and *in vivo* mechanistic studies, drug screening, and biomarker development. Its applications extend to disease modeling, where engineered variants help dissect mutations affecting its chaperone activity, and in gene therapy approaches aimed at boosting cellular protein quality control mechanisms. Overall, recombinant HSPB8 serves as a vital tool for both basic research and translational innovation.
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