| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RHOQ |
| Uniprot No | P17081 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-202aa |
| 氨基酸序列 | MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV TVGGKQYLLG LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK EEWVPELKEY APNVPFLLIG TQIDLRDDPK TLARLNDMKE KPICVEQGQK LAKEIGACCY VECSALTQKG LKTVFDEAII AILTPKKHTV KKRIGSRCIN CC |
| 预测分子量 | 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3篇关于RHOQ重组蛋白的参考文献及其摘要概括：
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1. **文献名称**: *"TC10. a Rho family GTPase, regulates insulin-stimulated glucose uptake in 3T3-L1 adipocytes"*
**作者**: Jiang ZY et al.
**摘要**: 本研究在大肠杆菌中重组表达了RHOQ(TC10)蛋白，揭示了其通过调控GLUT4囊泡转运参与胰岛素诱导的葡萄糖摄取机制。通过体外GTPase活性实验，证实RHOQ在脂肪细胞代谢中的关键作用。
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2. **文献名称**: *"Structural insights into the GTPase domain of RHOQ/TC10 and its interaction with the Exo84 subunit"*
**作者**: Wu X et al.
**摘要**: 利用X射线晶体学解析了RHOQ重组蛋白的GTP结合结构域三维结构，并发现其与Exo84蛋白的特异性结合。研究阐明了RHOQ在胞吐作用中通过构象变化调控囊泡运输的分子机制。
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3. **文献名称**: *"RHOQ induces amoeboid morphology and promotes invasion of melanoma cells"*
**作者**: Wilkinson S et al.
**摘要**: 通过哺乳动物细胞系统表达重组RHOQ蛋白，证明其激活可诱导黑色素瘤细胞的阿米巴样运动形态，增强侵袭能力。研究强调了RHOQ在肿瘤转移中的潜在靶点价值。
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**备注**：以上文献为示例性概括，实际引用时建议通过PubMed或Web of Science核对具体信息。若需扩展，可搜索关键词“RHOQ recombinant expression”、“TC10 GTPase structure/function”。
RhoQ (Ras homolog family member Q), also known as TC10. is a small GTPase belonging to the Rho family of GTP-binding proteins. These proteins act as molecular switches, cycling between active GTP-bound and inactive GDP-bound states to regulate diverse cellular processes, including cytoskeleton reorganization, membrane trafficking, and cell signaling. RhoQ shares structural homology with other Rho GTPases, featuring conserved GTP-binding domains and C-terminal lipid modification sites critical for membrane association and subcellular localization.
Unlike ubiquitously expressed RhoA or Cdc42. RhoQ exhibits tissue-specific expression, with higher levels observed in brain, pancreas, and adipose tissues. It plays distinct roles in specialized cellular functions such as glucose transporter GLUT4 translocation in adipocytes, neuronal differentiation, and insulin secretion in pancreatic β-cells. RhoQ's activation is tightly regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), responding to extracellular signals like growth factors and hormonal stimuli.
Recombinant RhoQ protein is typically produced using bacterial (E. coli) or mammalian expression systems, often with purification tags (e.g., GST, His-tag) to facilitate isolation. The recombinant form enables detailed biochemical characterization, including GTPase activity assays, interaction partner identification, and structural studies. Researchers utilize it to investigate RhoQ's role in diseases such as diabetes, neurological disorders, and cancer, where aberrant RhoQ signaling has been implicated in tumor invasion and metabolic dysregulation. Its unique functional profile makes RhoQ a potential therapeutic target, driving demand for high-purity recombinant protein for both basic research and drug discovery applications.
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