| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VAV3 |
| Uniprot No | Q9UKW4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-847aa |
| 氨基酸序列 | MEPWKQCAQWLIHCKVLPTNHRVTWDSAQVFDLAQTLRDGVLLCQLLNNLRAHSINLKEINLRPQMSQFLCLKNIRTFLTACCETFGMRKSELFEAFDLFDVRDFGKVIETLSRLSRTPIALATGIRPFPTEESINDEDIYKGLPDLIDETLVEDEEDLYDCVYGEDEGGEVYEDLMKAEEAHQPKCPENDIRSCCLAEIKQTEEKYTETLESIEKYFMAPLKRFLTAAEFDSVFINIPELVKLHRNLMQEIHDSIVNKNDQNLYQVFINYKERLVIYGQYCSGVESAISSLDYISKTKEDVKLKLEECSKRANNGKFTLRDLLVVPMQRVLKYHLLLQELVKHTTDPTEKANLKLALDAMKDLAQYVNEVKRDNETLREIKQFQLSIENLNQPVLLFGRPQGDGEIRITTLDKHTKQERHIFLFDLAVIVCKRKGDNYEMKEIIDLQQYKIANNPTTDKENKKWSYGFYLIHTQGQNGLEFYCKTKDLKKKWLEQFEMALSNIRPDYADSNFHDFKMHTFTRVTSCKVCQMLLRGTFYQGYLCFKCGARAHKECLGRVDNCGRVNSGEQGTLKLPEKRTNGLRRTPKQVDPGLPKMQVIRNYSGTPPPALHEGPPLQLQAGDTVELLKGDAHSLFWQGRNLASGEVGFFPSDAVKPCPCVPKPVDYSCQPWYAGAMERLQAETELINRVNSTYLVRHRTKESGEYAISIKYNNEAKHIKILTRDGFFHIAENRKFKSLMELVEYYKHHSLKEGFRTLDTTLQFPYKEPEHSAGQRGNRAGNSLLSPKVLGIAIARYDFCARDMRELSLLKGDVVKIYTKMSANGWWRGEVNGRVGWFPSTYVEEDE |
| 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. |
以下是关于VAV3重组蛋白的参考文献示例(注：部分内容为模拟示例，建议通过学术数据库验证具体文献)：
---
1. **标题**: "Expression and Purification of Recombinant VAV3 in E. coli for Functional Characterization"
**作者**: Tanaka K, et al.
**摘要**: 本研究利用大肠杆菌表达系统成功制备了重组VAV3蛋白，并通过亲和层析纯化。功能实验表明，重组VAV3在体外表现出特异性鸟嘌呤核苷酸交换因子(GEF)活性，能够激活Rho家族GTP酶(如Rac1)，为研究其在癌症信号通路中的作用提供了工具。
2. **标题**: "Structural Insights into the Oncogenic Mutant VAV3 Recombinant Protein"
**作者**: Smith J, et al.
**摘要**: 通过X射线晶体学解析了重组VAV3蛋白及其致癌突变体的三维结构，揭示了关键结构域(如DH结构域)的构象变化如何增强其GEF活性，为靶向VAV3的肿瘤治疗策略提供了分子基础。
3. **标题**: "Recombinant VAV3 Protein Promotes Neuronal Differentiation via MAPK/ERK Signaling"
**作者**: Chen L, et al.
**摘要**: 在哺乳动物细胞中表达并纯化重组VAV3蛋白，发现其通过激活MAPK/ERK通路促进神经干细胞分化为成熟神经元，提示VAV3在神经发育和退行性疾病中的潜在作用。
4. **标题**: "Development of a VAV3 Recombinant Protein-Based Screening Assay for Small Molecule Inhibitors"
**作者**: Müller R, et al.
**摘要**: 本研究利用重组VAV3蛋白建立高通量筛选平台，鉴定出多个抑制其GEF活性的小分子化合物，为开发抗癌药物提供了先导化合物。
---
**建议**：上述文献为示例性质，实际引用时请通过PubMed、Web of Science等平台以关键词“VAV3 recombinant protein”“VAV3 expression”或“VAV3 purification”检索最新研究，并核实作者及摘要准确性。
Vav3 recombinant protein is a engineered form of the VAV3 protein, a member of the VAV family of guanine nucleotide exchange factors (GEFs) that regulate Rho/Rac GTPases in intracellular signaling. First identified in the 1990s, VAV3 plays critical roles in cell proliferation, differentiation, adhesion, and immune responses through its activation of pathways like PI3K/AKT and MAPK/ERK. Structurally, it contains conserved domains including a Dbl homology (DH) domain for GEF activity, pleckstrin homology (PH) domain for membrane interaction, and a calponin homology (CH) domain for cytoskeletal regulation.
Recombinant VAV3 proteins are typically produced in bacterial (e.g., E. coli) or mammalian expression systems to enable functional studies. They preserve key domains necessary for interacting with upstream receptors (e.g., tyrosine kinases) and downstream effectors. Purification often involves affinity tags like His-tags followed by chromatography techniques. These proteins serve as essential tools for investigating signaling cascades in cancer biology, neurological disorders, and immune regulation. Notably, VAV3 dysregulation has been linked to tumorigenesis in prostate, breast, and gastric cancers, where its overexpression promotes metastasis and therapy resistance.
Researchers utilize VAV3 recombinant proteins to map phosphorylation events, screen inhibitors, and establish disease models. Recent studies explore its potential as a therapeutic target, particularly in cancers with aberrant VAV3 activation. Functional validation through enzymatic assays (e.g., GDP/GTP exchange measurements) and protein interaction analyses remains crucial for confirming bioactivity. As interest grows in GTPase-mediated signaling networks, VAV3 recombinant proteins continue to support both basic research and preclinical drug development efforts.
×
