| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | INSR |
| Uniprot No | P06213 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1011-1382aa |
| 氨基酸序列 | YVPDEWEVSR EKITLLRELG QGSFGMVYEG NARDIIKGEA ETRVAVKTVN ESASLRERIE FLNEASVMKG FTCHHVVRLL GVVSKGQPTL VVMELMAHGD LKSYLRSLRP EAENNPGRPP PTLQEMIQMA AEIADGMAYL NAKKFVHRDL AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMAPESLKD GVFTTSSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDQPDN CPERVTDLMR MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFHSEENK APESEELEME FEDMENVPLD RSSHCQREEA GGRDGGSSLG FKRSYEEHIP YTHMNGGKKN GRILTLPRSN PS |
| 预测分子量 | 70 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INSR(胰岛素受体)重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
1. **文献名称**：*"Expression and Purification of Functional Recombinant Human Insulin Receptor Ectodomain in HEK293 Cells"*
**作者**：Smith J, et al.
**摘要**：该研究描述了在HEK293细胞中高效表达并纯化具有生物活性的人胰岛素受体胞外域重组蛋白的方法，验证了其与胰岛素的结合能力及信号激活功能，为结构研究和药物筛选提供了工具。
2. **文献名称**：*"Structural Insights into Insulin Receptor Activation by Cryo-EM of Recombinant Full-Length Receptor Complexes"*
**作者**：Brown K, et al.
**摘要**：通过冷冻电镜技术解析了全长重组人胰岛素受体与胰岛素结合的复合物结构，揭示了受体激活的分子机制，为糖尿病治疗靶点的优化提供了结构基础。
3. **文献名称**：*"Development of a Recombinant Insulin Receptor Kinase Domain for High-Throughput Inhibitor Screening"*
**作者**：Lee S, et al.
**摘要**：研究报道了一种重组表达并纯化胰岛素受体激酶结构域的方法，成功应用于高通量抑制剂筛选，筛选出新型小分子化合物，可能用于胰岛素抵抗相关疾病治疗。
(注：以上文献信息为示例性质，实际引用时需核实具体文献来源及准确性。)
The insulin receptor (INSR) is a transmembrane receptor tyrosine kinase that plays a central role in regulating glucose homeostasis, lipid metabolism, and cell growth. Structurally, it consists of two extracellular α-subunits that bind insulin and two β-subunits spanning the membrane with intracellular tyrosine kinase activity. Upon insulin binding, INSR undergoes autophosphorylation and activates downstream signaling cascades, including the PI3K-AKT and MAPK pathways, which mediate metabolic and mitogenic responses. Dysregulation of INSR signaling is linked to diabetes, obesity, cancer, and neurodegenerative disorders.
Recombinant INSR proteins are engineered using expression systems (e.g., mammalian, insect cells) to produce functional domains for research and therapeutic applications. These proteins often include soluble extracellular α-subunits or kinase domain fragments, enabling studies on insulin-binding kinetics, receptor activation mechanisms, and drug discovery. Mammalian cell systems are preferred for generating full-length INSR with proper glycosylation and disulfide bonds critical for ligand binding and structural integrity. Recombinant INSR variants have been pivotal in elucidating insulin resistance mechanisms in type 2 diabetes and screening insulin mimetics. They also serve as tools to develop therapeutic antibodies or inhibitors targeting INSR in cancers with aberrant insulin signaling. Additionally, truncated forms are used in diagnostic assays to detect autoantibodies in type 1 diabetes. Advances in protein engineering, such as fusion tags or site-specific mutations, further enhance the solubility, stability, and functional characterization of recombinant INSR, bridging structural biology with translational medicine.
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