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| 纯度 | ＞90% by SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGF1 |
| Uniprot No | P05230 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 16-155aa |
| 氨基酸序列 | MFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAE SVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYIS KKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD |
| 预测分子量 | 16 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FGF1重组蛋白的参考文献示例(信息为示例性概括，具体文献需通过学术数据库核实)：
1. **"Recombinant FGF1 protects against myocardial ischemia-reperfusion injury via activation of the PI3K/Akt pathway"**
*作者：Suh JM et al. (2016)*
**摘要**：研究证明重组FGF1蛋白通过激活PI3K/Akt信号通路，减少心肌细胞凋亡并改善心脏功能，在缺血-再灌注损伤模型中具有心脏保护作用。
2. **"Systemic administration of recombinant FGF1 ameliorates hyperglycemia in diabetic mouse models"**
*作者：Gasser E et al. (2014)*
**摘要**：报道重组FGF1通过调控胰岛素敏感性和糖代谢通路，显著降低糖尿病小鼠模型的血糖水平，提示其作为糖尿病治疗药物的潜力。
3. **"Engineering a thermostable fibroblast growth factor 1 by site-directed mutagenesis"**
*作者：Bishop ET et al. (2018)*
**摘要**：通过定点突变技术改造FGF1重组蛋白，显著提高其热稳定性与体内半衰期，为开发长效FGF1药物提供新策略。
4. **"FGF1 structural determinants for heparan sulfate binding and signaling activity"**
*作者：Beenken A et al. (2012)*
**摘要**：解析FGF1重组蛋白与肝素/硫酸乙酰肝素结合的关键结构域，揭示其调控下游信号转导的分子机制，为靶向药物设计奠定基础。
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建议通过PubMed或Web of Science以“recombinant FGF1 protein”等关键词检索最新文献，获取具体研究数据。
Fibroblast Growth Factor 1 (FGF1), a member of the FGF protein family, plays critical roles in cellular processes such as proliferation, differentiation, angiogenesis, and tissue repair. Discovered in the 1970s, FGF1 is a non-secretory, heparin-binding protein that signals through FGF receptors (FGFRs) with heparan sulfate as a cofactor. Unlike other FGFs, FGF1 lacks a canonical signal peptide and is released via non-classical pathways, enabling autocrine/paracrine actions in stress or injury. Structurally, it features a β-trefoil fold common to FGFs, facilitating receptor binding and activation of downstream pathways like MAPK and PI3K/AKT.
Recombinant FGF1 is produced using genetic engineering (e.g., E. coli or mammalian systems) to ensure high purity and bioactivity. Its therapeutic potential spans wound healing, cardiovascular diseases, and metabolic disorders. Studies highlight its ability to promote tissue regeneration, improve glucose metabolism, and protect neurons. However, challenges include short half-life, instability, and off-target effects. Research focuses on engineered variants, delivery systems (nanoparticles, hydrogels), and hybrid molecules to enhance efficacy. While clinical applications remain experimental, FGF1 remains a promising candidate for regenerative medicine and disease modulation.
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