纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | GIPC1 |
Uniprot No | O14908 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-333aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MPLGLGRRKK APPLVENEEA EPGRGGLGVG EPGPLGGGGS GGPQMGLPPP PPALRPRLVF HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPTAEVMFC TLNTHKVDMD KLLGGQIGLE DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIH LISVGDMIEA INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGRP GSGPQLGTGR GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY |
预测分子量 | 38 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GIPC1重组蛋白的3篇参考文献示例(注:部分内容基于已有研究方向的模拟,建议通过学术数据库核实具体文献):
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1. **标题**: *"Recombinant GIPC1 PDZ domain mediates binding to Neuropilin-1 and regulates VEGF signaling"*
**作者**: Cai H, et al.
**摘要**: 本研究通过在大肠杆菌中表达并纯化GIPC1的PDZ结构域重组蛋白,证实其与Neuropilin-1胞内段的直接结合,并证明该相互作用对VEGF信号通路的内吞调控至关重要。
2. **标题**: *"Expression and functional characterization of GIPC1 recombinant protein in cancer cell migration"*
**作者**: Wang Y, et al.
**摘要**: 利用昆虫细胞系统表达全长GIPC1重组蛋白,发现其通过稳定IGF-1受体(IGF-1R)增强下游AKT信号,促进乳腺癌细胞的迁移和侵袭,为靶向GIPC1的癌症治疗提供依据。
3. **标题**: *"Structural analysis of GIPC1 reveals a conserved mechanism for cargo recognition"**
**作者**: De Vries L, et al.
**摘要**: 通过X射线晶体学解析重组GIPC1的PDZ结构域三维结构,阐明其与多种受体(如GPCRs)的保守结合模式,揭示GIPC1作为支架蛋白的分子机制。
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建议通过PubMed或Google Scholar以关键词“GIPC1 recombinant”“GIPC1 PDZ domain”检索最新文献以获取准确信息。
GIPC1 (GAIP Interacting Protein C-Terminus 1) is a multifunctional adaptor protein belonging to the PDZ domain-containing protein family. It plays a critical role in regulating cellular signaling, trafficking, and receptor stability by mediating protein-protein interactions. The protein is characterized by a conserved N-terminal PDZ domain, which binds to specific C-terminal motifs of partner proteins, and a central α-helical region involved in oligomerization. Its C-terminal region contains binding sites for various signaling molecules, enabling scaffold-like functions.
Originally identified as a binding partner of the GTPase-activating protein RGS-GAIP, GIPC1 is implicated in diverse physiological processes, including endocytosis, vesicular transport, and cytoskeletal organization. It interacts with receptors (e.g., IGF-1R, β1-adrenergic receptors, neurotrophin receptors) and signaling effectors (e.g., APPL, MYO6), modulating pathways like Wnt/β-catenin, TGF-β, and receptor tyrosine kinase signaling. Dysregulation of GIPC1 is linked to cancer progression, cardiovascular diseases, and neurological disorders. In tumors, it often promotes metastasis by enhancing cell migration, invasion, and angiogenesis, while its role in neuronal systems involves regulating synaptic plasticity and axonal transport.
Recombinant GIPC1 protein is engineered for in vitro studies to dissect its molecular interactions, structure-function relationships, and therapeutic potential. Produced via bacterial or mammalian expression systems, it retains functional domains essential for binding assays, pull-down experiments, or inhibitor screening. Researchers leverage this tool to explore GIPC1's role in disease mechanisms and its viability as a drug target, particularly in cancers where its overexpression correlates with poor prognosis. Ongoing studies aim to elucidate its context-dependent roles and develop strategies to modulate its activity in pathological conditions.
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