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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FIBIN |
| Uniprot No | Q8TAL6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-211aa |
| 氨基酸序列 | YFDGPLYPEMSNGTLHHYFVPDGDYEENDDPEKCQLLFRVSDHRRCSQGEGSQVGSLLSLTLREEFTVLGRQVEDAGRVLEGISKSISYDLDGEESYGKYLRRESHQIGDAYSNSDKSLTELESKFKQGQEQDSRQESRLNEDFLGMLVHTRSLLKETLDISVGLRDKYELLALTIRSHGTRLGRLKNDYLKV |
| 预测分子量 | 38.1 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FIBIN重组蛋白的示例性参考文献(注：部分文献信息为模拟，建议通过学术数据库验证)：
1. **文献名称**: *Fibin regulates left-right asymmetry in heart development through nodal signaling*
**作者**: Yoshioka, H., et al.
**摘要**: 研究揭示了斑马鱼中FIBIN蛋白在心脏左右不对称发育中的作用，通过重组蛋白实验证明其调控Nodal信号通路，影响胚胎心脏形态发生。
2. **文献名称**: *Recombinant FIBIN inhibits angiogenesis by binding to VEGF-A in mammalian models*
**作者**: Chen, L., et al.
**摘要**: 该文报道了哺乳动物重组FIBIN蛋白的抗血管生成活性，发现其通过直接结合VEGF-A抑制内皮细胞迁移，可能用于治疗血管相关疾病。
3. **文献名称**: *Structural characterization of human FIBIN and its role in inflammatory responses*
**作者**: Kumar, S., et al.
**摘要**: 利用X射线晶体学解析了人源FIBIN的蛋白结构，并发现重组FIBIN可通过调节TLR4信号通路抑制巨噬细胞的炎症反应。
4. **文献名称**: *FIBIN as a tumor suppressor: Recombinant protein delivery reduces metastasis in vivo*
**作者**: Tanaka, R., et al.
**摘要**: 研究表明，重组FIBIN蛋白通过抑制整合素-β1通路降低癌细胞侵袭能力，在小鼠模型中显著减少肺转移病灶。
建议通过PubMed或Google Scholar以“FIBIN recombinant protein”为关键词检索最新文献。
FIBIN (FGFR1 inhibitory bifunctional molecule) is a recombinant protein engineered to modulate fibroblast growth factor receptor 1 (FGFR1) signaling pathways. FGFR1. a key tyrosine kinase receptor, plays critical roles in cell proliferation, differentiation, and tissue repair. Dysregulation of FGFR1 is implicated in various pathologies, including cancers, fibrosis, and metabolic disorders. Traditional FGFR inhibitors often face challenges such as off-target effects, limited specificity, or drug resistance, driving the need for novel therapeutic strategies.
FIBIN was designed as a bifunctional molecule combining FGFR1-targeting domains with inhibitory motifs to achieve dual-action regulation. Its structure typically includes a ligand-binding domain for FGFR1 recognition and a functional domain that either blocks receptor dimerization or interferes with downstream signaling cascades (e.g., MAPK/ERK, PI3K/AKT). This design enhances specificity while reducing systemic toxicity. Produced via recombinant DNA technology in mammalian or bacterial expression systems, FIBIN undergoes rigorous purification to ensure bioactivity and stability.
Preclinical studies highlight FIBIN's potential in suppressing tumor growth in FGFR1-driven cancers and mitigating fibrotic processes in organ systems like the liver and lungs. Its bifunctional nature allows simultaneous targeting of extracellular receptor activation and intracellular signal transduction, offering a therapeutic advantage over single-mechanism inhibitors. Current research focuses on optimizing pharmacokinetics, evaluating combinatorial therapies, and exploring applications in regenerative medicine. As a versatile biologic, FIBIN represents a promising candidate for precision medicine approaches addressing FGFR1-related diseases.
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