| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP47 |
| Uniprot No | P50454 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-418aa |
| 氨基酸序列 | AEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENIL VSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSL SNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRS ALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKM VDNRGFMVTRSYTVGVMMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLI ILMPHHVEPLERLEKLLTKEQLKIWMGKMQKKAVAISLPKGVVEVTHDLQ KHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFELDTDGNPFDQ DIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRPKGDKMRDEL |
| 预测分子量 | 46 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HSP47重组蛋白的3篇参考文献及摘要概括：
1. **文献名称**：*"Production of recombinant human HSP47 and its collagen-binding activity in vitro"*
**作者**：Nagai N, Hosokawa M, et al.
**摘要**：研究报道了在大肠杆菌中高效表达并纯化人源HSP47重组蛋白的方法，通过体外实验证实其与胶原蛋白的特异性结合能力，为研究胶原代谢机制提供工具。
2. **文献名称**：*"Crystal structure of the collagen-binding domain of HSP47 from Rattus norvegicus"*
**作者**：Ito S, Nagata K
**摘要**：通过重组表达大鼠HSP47蛋白的胶原结合结构域，利用X射线晶体学解析其三维结构，揭示了HSP47与胶原多肽链结合的关键氨基酸位点及作用机制。
3. **文献名称**：*"Recombinant HSP47 modulates TGF-β1-induced fibrosis in human fibroblasts"*
**作者**：Hagiwara S, et al.
**摘要**：研究显示，外源性重组HSP47蛋白可抑制TGF-β1诱导的人成纤维细胞胶原过度分泌，提示其在抗纤维化治疗中的潜在应用价值。
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**注**：上述文献为示例，实际引用时建议通过PubMed或Web of Science核对具体信息。HSP47重组蛋白研究多聚焦于其与胶原的相互作用机制及疾病治疗应用。
HSP47 (Heat Shock Protein 47), also known as Serpin H1. is a stress-inducible molecular chaperone critical for collagen biosynthesis. As a member of the serine protease inhibitor (serpin) superfamily, it uniquely lacks protease inhibitory activity but specializes in binding to procollagen in the endoplasmic reticulum (ER). Its primary role involves stabilizing newly synthesized collagen polypeptides, ensuring proper folding, and preventing premature aggregation or degradation during post-translational modifications. HSP47 exhibits high specificity for collagen types I–V and is pH-sensitive, releasing collagen upon exposure to the acidic environment of the Golgi apparatus or extracellular space.
Recombinant HSP47 protein is engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production for research and therapeutic applications. Its recombinant form retains the ability to bind collagen through conserved structural domains, including a reactive center loop essential for chaperone activity. Studies utilize HSP47 recombinant protein to investigate collagen-related pathologies, such as fibrosis, cancer progression, and connective tissue disorders, where dysregulated collagen turnover contributes to disease mechanisms. It also serves as a tool to explore HSP47’s interactions with collagen-binding partners or inhibitors, aiding drug discovery efforts targeting fibrotic diseases.
In regenerative medicine, recombinant HSP47 supports tissue engineering by optimizing collagen matrix assembly. Its role in stress responses, including heat shock and oxidative stress, further links it to cellular adaptation pathways. Research continues to unravel its non-canonical functions, such as modulating inflammation and autophagy, highlighting its multifaceted biological significance.
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