| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IRS1 |
| Uniprot No | P35568 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 157-267aa |
| 氨基酸序列 | GPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPR |
| 预测分子量 | 60.3 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IRS1重组蛋白的3篇参考文献示例(注：文献信息为模拟示例，非真实存在)：
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1. **文献名称**：*Recombinant IRS1 Expression and Its Role in Insulin Signaling*
**作者**：Smith J, et al.
**摘要**：本研究通过大肠杆菌系统成功表达并纯化了重组人IRS1蛋白，验证了其在体外能够与胰岛素受体结合并激活下游PI3K/Akt信号通路，为研究胰岛素抵抗机制提供了工具。
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2. **文献名称**：*Structural Analysis of IRS1 Phosphorylation Domains Using Recombinant Protein*
**作者**：Lee H, et al.
**摘要**：利用昆虫细胞表达系统制备了重组IRS1酪氨酸磷酸化结构域，通过质谱和分子对接技术揭示了关键磷酸化位点对胰岛素信号传导的调控作用，为糖尿病药物靶点开发提供依据。
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3. **文献名称**：*Functional Characterization of IRS1 Mutants in Metabolic Disorders*
**作者**：Garcia R, et al.
**摘要**：通过哺乳动物细胞表达重组IRS1突变体，发现特定氨基酸位点的突变会降低其与胰岛素受体的相互作用能力，提示遗传变异可能导致2型糖尿病发病风险增加。
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如需真实文献，建议在PubMed或Google Scholar检索以下关键词：**"recombinant IRS1 protein"**, **"IRS1 expression purification"**, **"IRS1 functional analysis"**。
IRS1 (Insulin Receptor Substrate 1) is a critical adaptor protein in intracellular signaling pathways, primarily mediating responses to insulin and insulin-like growth factor 1 (IGF-1). Discovered in the early 1990s, IRS1 belongs to the IRS family of proteins (IRS1-IRS6) and plays a central role in metabolic regulation, cell growth, and survival. Structurally, it contains multiple tyrosine phosphorylation sites, a pleckstrin homology (PH) domain for membrane localization, and a phosphotyrosine-binding (PTB) domain that interacts with activated insulin/IGF-1 receptors. Upon receptor activation, IRS1 is recruited and phosphorylated, enabling it to dock downstream effectors like PI3K (phosphatidylinositol 3-kinase) and Grb2/SOS, which trigger pathways such as AKT/mTOR (regulating metabolism and growth) and MAPK (influencing proliferation and differentiation).
Dysregulation of IRS1 is implicated in insulin resistance, type 2 diabetes, and certain cancers. For example, reduced IRS1 expression or impaired phosphorylation disrupts glucose uptake, while overexpression in cancers may drive tumorigenesis. Recombinant IRS1 proteins, produced via expression systems like *E. coli* or mammalian cells, are essential tools for studying these mechanisms. They enable *in vitro* analysis of protein interactions, post-translational modifications (e.g., phosphorylation, serine hyperphosphorylation in insulin resistance), and functional assays in cell models. Researchers also use recombinant IRS1 to screen therapeutic compounds targeting insulin signaling or oncogenic pathways. Its recombinant form retains structural and functional fidelity, making it invaluable for both basic research and drug development.
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