| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VBP1 |
| Uniprot No | P61758 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-197aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAAVKDS CGKGEMATGN GRRLHLGIPE AVFVEDVDSF MKQPGNETAD TVLKKLDEQY QKYKFMELNL AQKKRRLKGQ IPEIKQTLEI LKYMQKKKES TNSMETRFLL ADNLYCKASV PPTDKVCLWL GANVMLEYDI DEAQALLEKN LSTATKNLDS LEEDLDFLRD QFTTTEVNMA RVYNWDVKRR NKDDSTKNKA |
| 预测分子量 | 25 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VBP1重组蛋白的3篇模拟参考文献示例(基于学术文献常见方向推测)：
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1. **文献名称**: "Expression and Purification of Recombinant VBP1 Protein for Structural Studies"
**作者**: Li, X., et al.
**摘要**: 该研究报道了在大肠杆菌中高效表达人源VBP1重组蛋白的优化方法，采用His标签亲和层析和凝胶过滤技术纯化，获得高纯度蛋白。纯化后的蛋白用于X射线晶体学分析，揭示了VBP1与HIF-1α结合的结构域特征。
2. **文献名称**: "VBP1 Recombinant Protein Modulates VHL-Mediated Ubiquitination in Renal Carcinoma Cells"
**作者**: Wang, Y., et al.
**摘要**: 通过体外表达VBP1重组蛋白，研究其与VHL蛋白的相互作用机制。实验表明，VBP1通过竞争性结合增强HIF-1α的稳定性，促进肾癌细胞中缺氧信号通路的激活，为靶向治疗提供依据。
3. **文献名称**: "Functional Characterization of Recombinant VBP1 in Zebrafish Embryogenesis"
**作者**: Smith, J., & Chen, R.
**摘要**: 利用重组VBP1蛋白在斑马鱼模型中研究其发育调控功能。结果显示，外源性VBP1蛋白通过调控Wnt信号通路影响胚胎体轴形成，提示其在早期发育中的关键作用。
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**注**：以上内容为模拟文献，实际研究中建议通过PubMed、Web of Science等平台以关键词“VBP1 recombinant protein”或“VBP1 protein interaction”检索最新文献。
**Background of VBP1 Recombinant Protein**
VBP1 (Vascular Biosynthetic Protein 1), also known as Vimentin Binding Protein 1 or PARK12. is a multifunctional protein encoded by the *VBP1* gene in humans. It serves as a co-chaperone in the cellular protein-folding machinery, primarily interacting with the HSP90 (Heat Shock Protein 90) complex to regulate the stability and function of client proteins. Structurally, VBP1 contains a von Hippel-Lindau (VHL) tumor suppressor protein-binding domain and a cytoskeleton-associated region, enabling its involvement in diverse cellular processes such as protein quality control, cytoskeletal organization, and intracellular signaling.
A key role of VBP1 is its interaction with microtubules and vimentin, linking chaperone activity to cytoskeletal dynamics. This interaction is critical for maintaining cell shape, motility, and division. Additionally, VBP1 participates in the Wnt/β-catenin signaling pathway by promoting the degradation of β-catenin, thereby modulating cell proliferation and differentiation. Dysregulation of VBP1 has been implicated in pathological conditions, including neurodegenerative diseases (e.g., Parkinson’s disease), cancer metastasis, and cardiovascular disorders. For instance, reduced VBP1 expression correlates with enhanced tumor invasiveness and poor prognosis in certain cancers.
Recombinant VBP1 protein is engineered for research applications, enabling in vitro studies of its chaperone functions, protein-protein interactions, and therapeutic potential. It is commonly expressed in *E. coli* or mammalian systems, ensuring proper post-translational modifications. Researchers utilize this tool to investigate molecular mechanisms underlying disease progression, screen for drug candidates targeting VBP1-associated pathways, or develop biomarkers for diagnostic purposes. Its versatility makes VBP1 recombinant protein a valuable resource in both basic and translational biomedical research.
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