首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HGF |
| Uniprot No | P14210 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-728aa |
| 氨基酸序列 | QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS |
| 预测分子量 | 80 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HGF重组蛋白的参考文献示例(内容为模拟概括，非真实文献)：
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1. **《Production and Characterization of Recombinant Human Hepatocyte Growth Factor》**
*作者：Yamamoto K, et al.*
**摘要**：研究描述了利用大肠杆菌表达系统高效生产重组人HGF(rhHGF)的方法，并通过质谱和生物活性实验验证了其结构与功能，证实其具有促进肝细胞增殖的能力。
2. **《Therapeutic Potential of Recombinant HGF in a Mouse Model of Liver Fibrosis》**
*作者：Matsumoto K, Nakamura T.*
**摘要**：在小鼠肝纤维化模型中，重组HGF蛋白显著抑制了胶原沉积并促进肝组织再生，表明其在治疗慢性肝病中的临床应用潜力。
3. **《Recombinant HGF Enhances Wound Healing by Activating Epithelial-Mesenchymal Transition》**
*作者：Clark RA, et al.*
**摘要**：通过体外和动物实验证明，重组HGF通过激活上皮-间质转化(EMT)通路加速皮肤伤口愈合，为开发新型创伤修复药物提供了依据。
4. **《Mechanistic Insights into HGF Receptor c-Met Activation by Recombinant HGF》**
*作者：Gherardi E, et al.*
**摘要**：利用晶体学和细胞信号分析，揭示了重组HGF蛋白与c-Met受体结合后诱导二聚化的分子机制，阐明了其促细胞迁移和存活的关键信号通路。
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注：以上文献为示例，实际引用时需核实真实文献信息及数据库来源(如PubMed、ScienceDirect等)。
Hepatocyte Growth Factor (HGF), also known as scatter factor (SF), is a pleiotropic cytokine initially identified for its role in liver regeneration. Discovered in the 1980s, HGF is primarily secreted by mesenchymal cells and acts on epithelial and endothelial cells through its receptor, c-Met tyrosine kinase. Structurally, HGF is a heterodimeric protein composed of a 69 kDa α-chain and a 34 kDa β-chain linked by disulfide bonds. The α-chain contains an N-terminal hairpin domain and four kringle domains critical for receptor binding, while the β-chain harbors a serine protease-like domain essential for signaling activation.
Recombinant HGF (rHGF) is produced using genetic engineering techniques in expression systems such as *E. coli*, yeast, or mammalian cells. Its production enables scalable, high-purity formulations for research and therapeutic applications. rHGF retains the biological activities of native HGF, including promoting cell proliferation, migration, survival, and morphogenesis. These properties make it a key player in tissue repair, organ development, and angiogenesis. Notably, rHGF has shown therapeutic potential in treating liver diseases, chronic wounds, and cardiovascular disorders by stimulating tissue regeneration.
In regenerative medicine, rHGF is explored for enhancing stem cell differentiation and organoid development. However, challenges persist in optimizing its stability, delivery methods, and minimizing off-target effects, particularly in cancer contexts where HGF/c-Met signaling can drive tumor progression. Current research focuses on engineered variants, fusion proteins, or targeted delivery systems to improve clinical efficacy. Despite these hurdles, rHGF remains a cornerstone molecule for understanding growth factor biology and developing innovative therapies for degenerative and injury-related conditions.
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