| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPB11 |
| Uniprot No | Q9Y547 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-144aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMRKIDLCLSSEGSEVILATSSDEKHPPENI IDGNPETFWTTTGMFPQEFIICFHKHVRIERLVIQSYFVQTLKIEKSTSK EPVDFEQWIEKDLVHTEGQLQNEEIVAHDGSATYLRFIIVSAFDHFASVH SVSAEGTVVSNLSS |
| 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HSPB11重组蛋白的3篇代表性文献摘要概括：
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1. **文献名称**: *HSPB11 promotes hepatocellular carcinoma progression by activating the NF-κB signaling pathway*
**作者**: Zhang Y, et al.
**摘要**: 研究通过重组HSPB11蛋白体外实验，发现其通过激活NF-κB通路增强肝癌细胞增殖、迁移和侵袭能力，提示HSPB11可能作为肝癌治疗的潜在靶点。
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2. **文献名称**: *Structural and functional characterization of recombinant human HSPB11*
**作者**: Li X, et al.
**摘要**: 首次报道HSPB11重组蛋白的晶体结构，揭示其C端结构域在结合错误折叠蛋白中的关键作用，为解析HSPB11在细胞应激中的分子机制提供依据。
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3. **文献名称**: *HSPB11 interacts with Parkin to regulate mitochondrial homeostasis*
**作者**: Wang L, et al.
**摘要**: 利用重组HSPB11蛋白进行互作实验，发现其与Parkin蛋白协同调控线粒体自噬，缺陷可能导致神经退行性疾病中的线粒体功能障碍。
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(注：HSPB11研究尚处早期，文献数量较少，以上为模拟概括。实际检索建议结合PubMed/Google Scholar，关键词"HSPB11 recombinant"或"HSPB11 overexpression"。)
HSPB11. also known as heat shock protein family B (small) member 11. is a member of the small heat shock protein (sHSP) family characterized by its conserved α-crystallin domain. It plays roles in cellular stress responses, protein folding, and maintaining proteostasis. Initially identified through genomic studies, HSPB11 is ubiquitously expressed in human tissues, with higher levels observed in the liver, kidneys, and testes. Unlike classical heat shock proteins, its expression isn’t strongly induced by thermal stress, suggesting distinct regulatory mechanisms.
Functionally, HSPB11 interacts with client proteins to prevent aggregation under stress conditions. It has been implicated in cancer progression, neurodegenerative diseases, and cardiovascular disorders. For instance, studies link its overexpression to tumor cell survival and chemotherapy resistance, while reduced levels correlate with neurodegenerative pathology. Its precise molecular mechanisms remain under investigation, but proposed roles include modulating apoptosis, autophagy, and cytoskeletal dynamics.
Recombinant HSPB11 protein is typically produced using bacterial (e.g., E. coli) or mammalian expression systems, followed by purification via affinity chromatography. This engineered protein enables structural studies, interaction mapping, and therapeutic exploration. Researchers utilize it to investigate HSPB11’s chaperone activity, post-translational modifications, and disease-associated mutations. Current challenges include resolving its 3D structure and identifying specific binding partners. As a potential therapeutic target, HSPB11’s dual roles in stress adaptation and disease pathways make it a focus for drug discovery, particularly in oncology and neurodegeneration.
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