首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IGF1 |
| 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. |
以下是关于IGF1重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *Recombinant human IGF-1 (rhIGF-1) for the treatment of muscle diseases*
**作者**: Bach LA, Møller J
**摘要**: 该研究探讨了重组人IGF-1在治疗肌肉萎缩和肌营养不良症中的潜力，通过动物模型验证了其促进肌肉细胞增殖和抑制凋亡的作用，并讨论了其临床转化中的挑战。
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2. **文献名称**: *IGF-1 in the clinic: Lessons from human genetics and therapeutic trials*
**作者**: Clemmons DR
**摘要**: 综述了IGF1重组蛋白在糖尿病、生长激素不敏感综合征等疾病中的临床试验结果，分析了其促进组织修复和代谢调节的机制，同时强调需关注长期使用可能引发的副作用(如肿瘤风险)。
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3. **文献名称**: *Engineering of a stable recombinant IGF-1 analog for cell culture applications*
**作者**: Li Y, et al.
**摘要**: 该研究通过基因工程优化重组IGF1蛋白的稳定性与生物活性，开发了一种新型长效突变体，显著提升了其在细胞培养基中促进干细胞分化的效能，为生物制造提供了新工具。
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**备注**：以上文献信息为示例性质，实际引用时需核对原文及数据库(如PubMed或Web of Science)以确保准确性。如需更具体领域(如癌症、糖尿病或衰老研究)的文献，可进一步补充说明。
**Background of Recombinant IGF1 Protein**
Insulin-like Growth Factor 1 (IGF1) is a small, 70-amino-acid polypeptide hormone structurally homologous to insulin. It plays a critical role in growth, development, and metabolism by mediating the effects of growth hormone (GH). Primarily synthesized in the liver, IGF1 circulates in the bloodstream bound to IGF-binding proteins (IGFBPs), which regulate its bioavailability. It exerts its biological functions by binding to the IGF1 receptor (IGF1R), activating downstream signaling pathways like PI3K-AKT and MAPK, which promote cell proliferation, differentiation, and survival.
Recombinant IGF1 is produced using genetic engineering techniques, typically in *E. coli* or mammalian cell systems. The process involves cloning the human *IGF1* gene into an expression vector, followed by transfection into host cells for protein production. Post-expression, the protein undergoes purification steps (e.g., chromatography) to ensure high purity and bioactivity. Recombinant technology enables scalable production of IGF1 with consistent quality, overcoming limitations of early extraction methods that relied on animal tissues.
Therapeutic and research applications of recombinant IGF1 are extensive. Clinically, it has been explored for treating growth disorders, such as severe primary IGF1 deficiency (e.g., Laron syndrome), and metabolic conditions like diabetes. In research, it is used to study cellular mechanisms in aging, neurodegeneration, muscle atrophy, and cancer, where dysregulated IGF1 signaling is implicated. Additionally, recombinant IGF1 has potential in regenerative medicine, aiding tissue repair and wound healing.
Despite its promise, challenges remain, including optimizing delivery methods, minimizing off-target effects, and addressing concerns about its role in cancer progression. Ongoing studies aim to refine IGF1-based therapies and explore engineered variants with improved specificity and safety profiles.
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