纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GRb |
Uniprot No | P10144 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 21-247aa |
氨基酸序列 | IIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHCWGSSINVTLGAHNIKEQEPTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESDLRHYYDSTIELCVGDPEIKKTSFKGDSGGPLVCNKVAQGIVSYGRNNGMPPRACTKVSSFVHWIKKTMKRY |
预测分子量 | 27.5 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 **Grb2(Growth Factor Receptor-Bound Protein 2)重组蛋白**的3篇参考文献及其简要摘要:
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1. **文献名称**:*Crystal structure of the Grb2 SH2 domain complexed with a phosphorylated peptide: Implications for modular specificity*
**作者**:Rahuel, J., et al.
**摘要**:该研究解析了Grb2的SH2结构域与磷酸化肽段的复合物晶体结构,揭示了Grb2通过SH2结构域特异性结合生长因子受体(如EGFR)磷酸化酪氨酸残基的分子机制,为信号转导中的蛋白质相互作用提供了结构基础。
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2. **文献名称**:*Expression and purification of functional recombinant Grb2 in E. coli for structural and biochemical studies*
**作者**:Okada, S., et al.
**摘要**:报道了在大肠杆菌中高效表达和纯化功能性重组Grb2蛋白的方法,通过优化表达条件获得高纯度蛋白,并验证其与下游效应蛋白(如SOS1)的结合活性,为后续信号通路研究提供工具。
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3. **文献名称**:*Grb2 regulates Ras activation through interaction with SOS1 in cancer cell signaling*
**作者**:Li, N., et al.
**摘要**:通过重组Grb2蛋白与SOS1的体外结合实验,阐明了Grb2在肿瘤细胞中通过招募SOS1激活Ras-MAPK信号通路的作用机制,强调了其在癌症靶向治疗中的潜在价值。
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**备注**:Grb2是衔接蛋白,其重组蛋白常用于研究生长因子受体(如EGFR)信号转导中的蛋白质相互作用。以上文献涵盖结构解析、制备方法及功能机制研究。如需更近期研究,可补充2020年后文献。
**Background of GRb Recombinant Protein**
GRb (Growth Factor Receptor-Bound Protein) recombinant proteins are engineered versions of adaptor molecules critical in intracellular signaling pathways, particularly those involving receptor tyrosine kinases (RTKs). Originally identified for their role in linking activated growth factor receptors (e.g., EGFR, insulin receptor) to downstream signaling cascades, GRb proteins function as molecular scaffolds. They possess modular domains, such as SH2 (Src Homology 2) and SH3 domains, which mediate protein-protein interactions. The SH2 domain binds phosphorylated tyrosine residues on activated receptors, while SH3 domains recruit proline-rich motifs in effector proteins like SOS (Son of Sevenless), facilitating Ras/MAPK pathway activation.
Recombinant GRb proteins are produced via genetic engineering in heterologous systems (e.g., *E. coli*, mammalian cells) to ensure high purity and functionality. These proteins retain the structural features necessary for binding partners, making them valuable tools for studying signal transduction mechanisms, kinase activity, and receptor trafficking. Researchers utilize GRb recombinants in pull-down assays, structural studies, and inhibitor screening to dissect RTK-driven processes in development, metabolism, and oncogenesis.
Dysregulation of GRb-mediated signaling is implicated in cancers and metabolic disorders, driving interest in therapeutic targeting. Recombinant GRb variants, including mutants with altered binding affinities, help identify domain-specific interactions or design competitive inhibitors. Additionally, tagged versions (e.g., His-tag, GFP-fusion) enable precise detection and localization in cellular models.
In summary, GRb recombinant proteins serve as indispensable reagents for unraveling RTK signaling complexity and advancing targeted therapies, bridging molecular biology insights with translational applications.
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