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 | Igfl |
| Uniprot No | P05019 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 49-118aa |
| 氨基酸序列 | GP ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSA |
| 预测分子量 | 8 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. |
以下为3篇关于IGF-1(胰岛素样生长因子1)重组蛋白的示例参考文献(注：文献标题与作者为虚构示例，实际研究请通过学术数据库检索)：
1. **《Recombinant Human IGF-1 Promotes Neuronal Cell Survival in vitro》**
- 作者：Smith J, et al.
- 摘要：研究证明重组人IGF-1蛋白通过激活PI3K/Akt信号通路，显著增强体外培养的神经元细胞存活率，提示其在神经退行性疾病中的潜在治疗价值。
2. **《Engineering a Long-Acting IGF-1 Fusion Protein for Diabetes Therapy》**
- 作者：Chen L, et al.
- 摘要：开发了一种与白蛋白融合的重组长效IGF-1蛋白，动物实验显示其可改善胰岛素敏感性并降低血糖水平，为糖尿病治疗提供新策略。
3. **《IGF-1-Loaded Nanoparticles Enhance Skeletal Muscle Regeneration》**
- 作者：Kim S, et al.
- 摘要：通过纳米颗粒递送重组IGF-1至损伤肌肉组织，实验证明其可加速肌纤维再生并减少炎症反应，为运动损伤修复提供新方法。
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如需真实文献，建议通过 **PubMed(https://pubmed.ncbi.nlm.nih.gov)** 检索关键词：
`recombinant IGF-1 protein therapeutic application`
或限定领域如：`IGF-1 tissue engineering` / `IGF-1 drug delivery`
**Background of Recombinant IgFL Protein**
The IgFL (Immunoglobulin-like Fibronectin Type III and Leucine-rich repeat) protein family comprises multifunctional molecules characterized by structural domains involved in cell adhesion, signaling, and extracellular matrix interactions. These proteins typically contain immunoglobulin (Ig) domains, fibronectin type III (FN3) repeats, and leucine-rich repeats (LRRs), which facilitate protein-protein interactions critical for cellular communication. IgFL members are implicated in diverse physiological processes, including tissue development, immune regulation, and neuronal connectivity.
Recombinant IgFL proteins are engineered using biotechnological platforms, such as *E. coli*, yeast, or mammalian expression systems*, to produce purified, bioactive forms for research and therapeutic applications. The recombinant approach allows precise control over protein folding, post-translational modifications, and scalability. For instance, mammalian systems (e.g., CHO cells) are preferred for producing glycosylated IgFL variants to mimic native functionality.
Functionally, IgFL proteins often act as ligands or co-receptors for cell surface receptors, modulating pathways like Wnt, TGF-β, or receptor tyrosine kinases. Their roles in cell proliferation, differentiation, and apoptosis have spurred interest in regenerative medicine and cancer therapy. For example, recombinant IgFL variants are explored for tissue repair by enhancing stem cell survival or for inhibiting tumor growth via receptor antagonism.
Challenges in IgFL recombinant production include maintaining structural integrity and avoiding aggregation. Advanced purification techniques (e.g., affinity chromatography) and structural optimization (e.g., truncation variants) address these issues. Current research focuses on tailoring IgFL proteins for targeted drug delivery, immunotherapies, and biomaterial coatings, highlighting their versatility in bridging structural biology and translational medicine.
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