| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RHOV |
| Uniprot No | Q96L33 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-236aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMPPRELS EAEPPPLRAP TPPPRRRSAP PELGIKCVLV GDGAVGKSSL IVSYTCNGYP ARYRPTALDT FSVQVLVDGA PVRIELWDTA GQEDFDRLRS LCYPDTDVFL ACFSVVQPSS FQNITEKWLP EIRTHNPQAP VLLVGTQADL RDDVNVLIQL DQGGREGPVP QPQAQGLAEK IRACCYLECS ALTQKNLKEV FDSAILSAIE HKARLEKKLN AKGVRTLSRC RWKKFFCFV |
| 预测分子量 | 29 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篇与RHOV重组蛋白相关的文献概览(注：RHOV相关研究相对较少，以下为模拟示例)：
1. **标题**：RHOV promotes keratinocyte cell migration by regulating actin dynamics through interaction with IQGAP1
**作者**：Moriyama, K., et al.
**摘要**：该研究通过重组RHOV蛋白体外实验，发现其与IQGAP1相互作用，调控肌动蛋白重组并促进皮肤角质形成细胞迁移，提示RHOV在伤口愈合中的作用。
2. **标题**：Crystal structure and biochemical characterization of the GTPase domain of RHOV
**作者**：Zhang, Y., et al.
**摘要**：解析了RHOV GTP酶结构域的重组蛋白晶体结构(PDB: 6T2X)，揭示了其与Rho家族其他成员(如RhoA)的活性位点差异，为靶向抑制剂设计提供依据。
3. **标题**：RHOV regulates melanoma invasion via reactive oxygen species-dependent mechanism
**作者**：Feng, X., et al.
**摘要**：利用原核表达的重组RHOV蛋白进行体外侵袭实验，证明其通过激活ROS信号通路增强黑色素瘤细胞侵袭能力，提示RHOV作为癌症治疗潜在靶点。
注：实际文献需通过PubMed/Google Scholar检索确认，建议使用关键词 "RHOV recombinant protein" 或 "RHOV GTPase" 获取最新研究。部分研究可能未直接使用重组蛋白，但涉及RHOV功能机制。
RHOV (Ras homolog family member V), also known as RhoV or Chp/Wrch-2. is a small GTPase belonging to the Rho family of proteins, which are critical regulators of cytoskeletal dynamics, cell migration, and signal transduction. Unlike classical Rho GTPases (e.g., RhoA, Rac1. Cdc42), RHOV exhibits unique structural features, including a divergent C-terminal region and altered effector-binding domains, suggesting specialized functional roles. It was initially identified as a developmentally regulated gene in vertebrates, with elevated expression in neural crest-derived tissues, skin, and certain cancers.
RHOV functions as a molecular switch, cycling between active GTP-bound and inactive GDP-bound states. It interacts with specific guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) to regulate downstream pathways, particularly those involving actin reorganization and cell adhesion. Studies implicate RHOV in diverse biological processes, including neurite outgrowth, keratinocyte differentiation, and immune cell activation. Notably, its dysregulation has been associated with tumor progression, metastasis, and drug resistance in cancers like melanoma and breast cancer.
Recombinant RHOV protein is engineered using expression systems (e.g., E. coli, mammalian cells) to study its biochemical properties, structure-function relationships, and interactions. Purification typically involves affinity tags (e.g., His-tag) followed by chromatography. This recombinant tool enables in vitro assays to characterize GTPase activity, screen inhibitors, or map protein interaction networks. Challenges in RHOV research include its low endogenous expression, overlapping functions with other Rho GTPases, and context-dependent signaling outcomes. Current efforts focus on elucidating its tissue-specific roles and therapeutic potential in diseases linked to cytoskeletal dysregulation.
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