| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGF12 |
| Uniprot No | P61328 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-181aa |
| 氨基酸序列 | MESKEPQLKGIVTRLFSQQGYFLQMHPDGTIDGTKDENSDYTLFNLIPVG LRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSST LYRQQESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVCMYREQS LHEIGEKQGRSRKSSGTPTMNGGKVVNQDST |
| 预测分子量 | 21 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FGF12重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**：*Structural and functional analysis of FGF12 using recombinant protein expression*
**作者**：Wang Y, et al.
**摘要**：该研究通过大肠杆菌系统成功表达并纯化了重组FGF12蛋白，利用核磁共振(NMR)技术解析其三维结构，揭示了其与钠离子通道相互作用的特定结构域，为FGF12在神经系统电信号调控中的机制提供了分子基础。
2. **文献名称**：*FGF12 recombinant protein modulates cardiac ion channels and arrhythmia susceptibility*
**作者**：Hennessey JA, et al.
**摘要**：作者通过哺乳动物细胞表达系统制备重组FGF12蛋白，发现其可调控心肌细胞电压门控钠通道(Nav1.5)的功能，并证实FGF12异常表达与心律失常相关，为心脏疾病的治疗提供了潜在靶点。
3. **文献名称**：*Recombinant FGF12 promotes neuronal regeneration via FGFR signaling*
**作者**：Liu X, et al.
**摘要**：研究采用昆虫细胞表达系统生产高活性重组FGF12蛋白，体外实验表明其通过激活FGFR1受体促进神经元轴突再生，提示FGF12在神经损伤修复中的治疗潜力。
(注：以上文献信息为示例，实际文献需通过学术数据库检索确认。)
Fibroblast Growth Factor 12 (FGF12) is a member of the fibroblast growth factor family, which comprises 22 signaling proteins involved in cell proliferation, differentiation, and tissue repair. Unlike canonical FGFs (e.g., FGF1. FGF2), FGF12 belongs to the FGF11 subfamily (FGF11-14), characterized by intracellular localization and lack of secretory signals. These "hormone-like" FGFs function independently of cell surface receptors, primarily modulating ion channels and synaptic activity through protein-protein interactions.
Structurally, FGF12 contains conserved β-trefoil domains but lacks heparin-binding regions critical for extracellular signaling. It interacts with voltage-gated sodium channels (Nav) and scaffolding proteins, regulating neuronal excitability and cardiac electrophysiology. Alternative splicing generates multiple isoforms (e.g., FGF12A, FGF12B) with distinct tissue distributions and functions, particularly in the nervous system and heart.
Recombinant FGF12 proteins are typically produced using bacterial (E. coli) or mammalian expression systems, followed by affinity chromatography purification. Engineered tags (e.g., His-tag) facilitate isolation while maintaining functional integrity. Recombinant forms enable detailed studies of FGF12's structure-function relationships, particularly its role in neurological disorders (epilepsy, neuropathic pain) and cardiovascular diseases (arrhythmias). Researchers also explore its potential as a therapeutic target or biomarker, though challenges persist in understanding its context-dependent signaling crosstalk and isoform-specific effects. Recent studies highlight its involvement in neuroprotection and cardiac remodeling, driving interest in developing modulators for precision medicine applications.
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