| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP27 |
| Uniprot No | Q16082 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-182aa |
| 氨基酸序列 | MSGRSVPHAHPATAEYEFANPSRLGEQRFGEGLLPEEILTPTLYHGYYVRPRAAPAGEGSRAGASELRLSEGKFQAFLDVSHFTPDEVTVRTVDNLLEVSARHPQRLDRHGFVSREFCRTYVLPADVDPWRVRAALSHDGILNLEAPRGGRHLDTEVNEVYISLLPAPPDPEEEEEAAIVEP |
| 预测分子量 | 47.2kDa |
| 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HSP27重组蛋白的3篇文献参考(内容基于公开研究概括，非真实文献)：
1. **文献名称**：*Recombinant HSP27 Protein Attenuates Oxidative Stress in Neuronal Cells*
**作者**：Smith J, et al.
**摘要**：研究利用大肠杆菌表达系统纯化重组人HSP27蛋白，证明其能通过抑制ROS生成显著减少神经细胞在氧化应激下的损伤，提示其在神经退行性疾病中的潜在治疗价值。
2. **文献名称**：*HSP27 Recombinant Protein Enhances Cellular Survival via Apoptosis Regulation*
**作者**：Chen L, Wang H.
**摘要**：通过体外实验发现，重组HSP27蛋白通过调控Bcl-2家族蛋白表达，抑制Caspase-3激活，从而减少化疗药物诱导的肿瘤细胞凋亡，揭示其在癌症耐药性中的作用机制。
3. **文献名称**：*Expression and Purification of Functional HSP27 in a Baculovirus System*
**作者**：Kumar R, et al.
**摘要**：报道了一种利用昆虫杆状病毒系统高效表达重组HSP27的方法，纯化后的蛋白具有分子伴侣活性，可恢复热应激下错误折叠蛋白的稳定性，为工业级制备提供新策略。
(注：以上为模拟示例，实际文献需通过PubMed/Google Scholar检索关键词“recombinant HSP27”获取。)
Heat shock protein 27 (HSP27), also known as HSPB1. is a member of the small heat shock protein (sHSP) family, characterized by its low molecular weight (~27 kDa) and conserved α-crystallin domain. It functions as a molecular chaperone, assisting in protein folding, preventing aggregation of denatured proteins, and promoting cellular survival under stress conditions such as heat shock, oxidative stress, or chemical toxicity. HSP27 is constitutively expressed at low levels in many tissues but is highly upregulated in response to cellular stress through the heat shock factor (HSF)-mediated pathway.
Recombinant HSP27 is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to ensure proper post-translational modifications, particularly phosphorylation. Phosphorylation at serine residues (e.g., Ser-15. Ser-78. Ser-82) regulates its oligomerization state and chaperone activity. In its unphosphorylated form, HSP27 forms large oligomers that act as a storage state, while phosphorylation triggers dissociation into smaller, active subunits with enhanced chaperone function.
Research on recombinant HSP27 has highlighted its dual role in diseases. It exhibits cytoprotective effects in neurodegenerative disorders (e.g., Alzheimer’s, Parkinson’s) by mitigating protein aggregation and apoptosis. Conversely, it is implicated in cancer progression, where overexpression in tumors correlates with therapy resistance and poor prognosis, likely due to its anti-apoptotic and metastasis-promoting properties. Additionally, HSP27 interacts with key signaling pathways, including NF-κB and AKT, influencing inflammation, cytoskeletal dynamics, and autophagy.
In biomedical applications, recombinant HSP27 is used to study stress response mechanisms, screen potential therapeutics targeting HSP27-associated pathways, and explore its diagnostic potential as a biomarker in conditions like cancer and cardiovascular diseases. Its structural flexibility and functional versatility make it a critical subject in both basic research and translational medicine.
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