纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GIPC2 |
Uniprot No | Q8TF65 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-315aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMPLKLR GKKKAKSKET AGLVEGEPTG AGGGSLSASR APARRLVFHA QLAHGSATGR VEGFSSIQEL YAQIAGAFEI SPSEILYCTL NTPKIDMERL LGGQLGLEDF IFAHVKGIEK EVNVYKSEDS LGLTITDNGV GYAFIKRIKD GGVIDSVKTI CVGDHIESIN GENIVGWRHY DVAKKLKELK KEELFTMKLI EPKKAFEIEP RSKAGKSSGE KIGCGRATLR LRSKGPATVE EMPSETKAKA IEKIDDVLEL YMGIRDIDLA TTMFEAGKDK VNPDEFAVAL DETLGDFAFP DEFVFDVWGV IGDAKRRGL |
预测分子量 | 37 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GIPC2重组蛋白的3篇代表性文献的简要总结(基于现有研究主题虚构示例,实际文献需通过数据库检索确认):
1. **"GIPC2 regulates insulin signaling through interaction with IGF-1R"**
*Authors: Lee S, et al.*
摘要:研究报道GIPC2重组蛋白通过PDZ结构域与胰岛素样生长因子1受体(IGF-1R)结合,调控下游PI3K/AKT信号通路,提示其在代谢疾病中的潜在作用。
2. **"Structural characterization of recombinant GIPC2 and its role in neuronal trafficking"**
*Authors: Müller T, et al.*
摘要:通过大肠杆菌表达系统获得高纯度GIPC2重组蛋白,解析其三维结构并发现其参与神经细胞囊泡运输的功能,为神经退行性疾病研究提供新靶点。
3. **"GIPC2 as a biomarker in pancreatic cancer: Recombinant protein-based analysis"**
*Authors: Chen H, et al.*
摘要:利用重组GIPC2蛋白开发ELISA检测方法,发现其在胰腺癌患者血清中显著高表达,提示其作为新型肿瘤标志物的临床潜力。
**备注**:以上文献为模拟示例,实际研究需通过PubMed、Google Scholar等平台以关键词"GIPC2 recombinant protein"或"GIPC2 structure/function"检索真实文献。GIPC2相关研究多集中于癌症、代谢调控及受体互作机制领域。
**Background of GIPC2 Recombinant Protein**
GIPC2 (GAIP-interacting protein C-terminus 2) belongs to the GIPC family of PDZ domain-containing proteins, which play critical roles in regulating transmembrane receptor trafficking, signal transduction, and cellular processes such as proliferation, adhesion, and apoptosis. Structurally, GIPC2 features a central PDZ domain that mediates interactions with the cytoplasmic tails of various receptors (e.g., integrins, GPCRs) and a C-terminal coiled-coil domain involved in oligomerization. This modular design enables GIPC2 to act as a scaffolding protein, bridging receptors with downstream signaling effectors or trafficking machinery.
GIPC2 is implicated in diverse physiological and pathological contexts. Studies highlight its involvement in cancer progression, where it modulates pathways like Wnt/β-catenin and TGF-β, influencing tumor growth, metastasis, and drug resistance. For instance, GIPC2 downregulation is associated with poor prognosis in hepatocellular carcinoma, while its overexpression suppresses colorectal cancer invasion. Beyond oncology, GIPC2 interacts with neurodevelopmental receptors (e.g., DCC, IGF-1R), suggesting roles in neuronal guidance and metabolism.
Recombinant GIPC2 protein, produced via heterologous expression systems (e.g., *E. coli*, mammalian cells), retains functional domains for *in vitro* studies. It serves as a tool to investigate protein-protein interactions, receptor internalization, or signaling mechanisms. Its therapeutic potential is being explored, particularly in cancers where restoring GIPC2 expression may counteract oncogenic pathways. However, its pleiotropic functions and tissue-specific roles necessitate further research to clarify context-dependent mechanisms and validate clinical relevance. Overall, GIPC2 represents a promising yet understudied target for understanding disease biology and developing precision therapies.
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