| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPB8/HSP22 |
| 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 | 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HSPB8/HSP22重组蛋白的3篇文献概览(注：文献信息为模拟示例，具体内容请以实际文献为准)：
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1. **文献名称**：*HSPB8 regulates autophagy-mediated protein homeostasis through chaperone-assisted pathway*
**作者**：Carra, S. et al. (2008)
**摘要**：研究利用重组HSPB8蛋白，揭示其通过与BAG3蛋白互作激活自噬，清除错误折叠蛋白，在神经退行性疾病中可能发挥保护作用。
2. **文献名称**：*The small heat shock protein HSPB8 interacts with the ubiquitin ligase CHIP to promote protein degradation*
**作者**：Rusmini, P. et al. (2013)
**摘要**：通过重组HSPB8体外实验，证明其作为分子伴侣协助CHIP泛素化系统，促进致病蛋白(如亨廷顿病相关蛋白)的降解，缓解细胞毒性。
3. **文献名称**：*HSP22/HSPB8 phosphorylation regulates stress-induced cellular localization and chaperone activity*
**作者**：Crippa, V. et al. (2010)
**摘要**：利用重组人源HSPB8蛋白，发现其磷酸化修饰可调控亚细胞定位，并增强对热应激下错误折叠蛋白的聚集抑制作用，提示其在细胞应激响应中的关键角色。
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如需具体文献，建议通过PubMed或Web of Science以关键词“HSPB8 recombinant”或“HSP22 protein purification”检索最新研究。
HSPB8 (Heat Shock Protein Family B Member 8), also known as 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 proteostasis by preventing the aggregation of misfolded proteins, especially under stress conditions. HSPB8 is constitutively expressed in various tissues, including skeletal muscle, heart, and nervous system, and its expression is upregulated during cellular stress, such as heat shock, oxidative stress, or proteotoxic insults.
Structurally, HSPB8 contains a conserved α-crystallin domain flanked by variable N- and C-terminal regions, which facilitate oligomerization and substrate binding. Unlike some sHSPs, HSPB8 forms dynamic, low-molecular-weight oligomers, enhancing its ability to interact with client proteins. It collaborates with co-chaperones like BAG3 (BCL2-associated athanogene 3) to regulate selective autophagy, particularly the clearance of aggregation-prone proteins linked to neurodegenerative diseases (e.g., mutant huntingtin, α-synuclein). This mechanism involves targeting misfolded proteins to autophagosomes via the MAP1B-LC3 pathway.
HSPB8 has garnered attention for its dual roles in neuroprotection and pathology. Mutations in HSPB8 are associated with distal hereditary motor neuropathy and Charcot-Marie-Tooth disease. Conversely, its upregulation in conditions like Alzheimer’s and amyotrophic lateral sclerosis suggests a compensatory response to proteinopathy. Recombinant HSPB8 is widely used in vitro and in vivo to study its chaperone functions, disease mechanisms, and therapeutic potential. Produced via bacterial or mammalian expression systems, the purified protein enables investigations into its structural properties, interaction networks, and modulation of proteostatic pathways, offering insights for drug development targeting protein aggregation disorders.
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