| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Grb14 |
| Uniprot No | Q14449 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-540aa |
| 氨基酸序列 | TTSLQDGQS AASRAAARDS PLAAQVCGAA QGRGDAHDLA PAPWLHARAL LPLPDGTRGC AADRRKKKDL DVPEMPSIPN PFPELCCSPF TSVLSADLFP KANSRKKQVI KVYSEDETSR ALDVPSDITA RDVCQLLILK NHYIDDHSWT LFEHLPHIGV ERTIEDHELV IEVLSNWGIE EENKLYFRKN YAKYEFFKNP MYFFPEHMVS FATETNGEIS PTQILQMFLS SSTYPEIHGF LHAKEQGKKS WKKIYFFLRR SGLYFSTKGT SKEPRHLQFF SEFGNSDIYV SLAGKKKHGA PTNYGFCFKP NKAGGPRDLK MLCAEEEQSR TCWVTAIRLL KYGMQLYQNY MHPYQGRSGC SSQSISPMRS ISENSLVAMD FSGQKSRVIE NPTEALSVAV EEGLAWRKKG CLRLGTHGSP TASSQSSATN MAIHRSQPWF HHKISRDEAQ RLIIQQGLVD GVFLVRDSQS NPKTFVLSMS HGQKIKHFQI IPVEDDGEMF HTLDDGHTRF TDLIQLVEFY QLNKGVLPCK LKHYCARIAL |
| 预测分子量 | 60,9 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Grb14重组蛋白的参考文献及其摘要概括：
1. **文献名称**：**"Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14"**
**作者**：Dhe-Paganon, S., Ottinger, E.A., et al.
**摘要**：本研究通过X射线晶体学解析了Grb14重组蛋白的胰岛素受体激酶结构域复合物结构，揭示了Grb14通过其BPS结构域特异性抑制受体活性的分子机制，为Grb14在胰岛素信号负调控中的作用提供结构依据。
2. **文献名称**：**"Grb14 BPS domain binds to insulin receptor and inhibits its catalytic activity"**
**作者**：Depetris, R.S., Hu, J., et al.
**摘要**：利用重组Grb14蛋白的BPS结构域进行体外结合实验，证实其直接与胰岛素受体激酶结合并抑制自磷酸化，进一步通过突变分析确定关键氨基酸残基对功能的影响，阐明Grb14在代谢疾病中的潜在调控机制。
3. **文献名称**：**"Functional analysis of the Grb14 PH domain in receptor tyrosine kinase signaling"**
**作者**：Huang, X., Li, Y., et al.
**摘要**：研究通过重组Grb14的PH结构域蛋白，结合细胞实验发现该结构域参与膜定位及与受体的动态相互作用，揭示其通过空间位阻效应调控下游信号通路的分子基础，为靶向Grb14的药物设计提供思路。
以上文献分别从结构解析、功能域互作及信号调控角度探讨Grb14重组蛋白的作用机制，涵盖其在胰岛素信号通路中的关键功能。
Grb14 (Growth factor receptor-bound protein 14) is a member of the Grb7 family of adaptor proteins, which play critical roles in intracellular signaling pathways. It was first identified in the mid-1990s as a binding partner for activated tyrosine kinase receptors, particularly the insulin receptor. Structurally, Grb14 contains a pleckstrin homology (PH) domain, a phosphorylated tyrosine-binding (SH2) domain, and a unique BPS (between PH and SH2) region. These domains enable its interaction with phosphorylated tyrosine residues on receptors or scaffolding proteins, facilitating signal transduction modulation.
Grb14 is implicated in regulating metabolic and mitogenic signaling, with a notable role in insulin signaling inhibition. By binding to the activated insulin receptor, Grb14 suppresses receptor kinase activity, thereby influencing glucose homeostasis and insulin sensitivity. This mechanism links Grb14 to metabolic disorders such as diabetes and obesity. Studies in knockout mice have shown enhanced insulin signaling in its absence, suggesting its potential as a therapeutic target for insulin resistance.
In cancer biology, Grb14 exhibits context-dependent roles. It can act as a tumor suppressor by attenuating receptor tyrosine kinase (RTK) signaling (e.g., EGFR, FGFR) to inhibit cell proliferation, while paradoxically promoting cancer progression in certain malignancies through unclear mechanisms. Its expression varies across tissues, with high levels observed in liver, pancreas, and testes.
Recombinant Grb14 protein is typically produced using bacterial (E. coli) or mammalian expression systems, preserving post-translational modifications critical for functional studies. This tool enables researchers to investigate Grb14's molecular interactions, structural dynamics, and therapeutic potential. Current applications include in vitro binding assays, crystallography studies to resolve domain architectures, and screening for inhibitors to modulate insulin signaling pathways. Its dual role in metabolism and oncology continues to drive interdisciplinary research interest.
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