| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VPRBP |
| Uniprot No | Q9Y4B6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1045-1396aa |
| 氨基酸序列 | QAPINFTSRLNRRASFPKYGGVDGGCFDRHLIFSRFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVPALDQCRVVFNHTGTVMYGAMLQADDEDDLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQGSMDALNMDTVCRLYEVGRQRLAE |
| 预测分子量 | 46.0 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VPRBP重组蛋白的3篇代表性文献摘要概括：
1. **文献名称**：*"Recombinant VPRBP protein expression and its role in cell cycle regulation"*
**作者**：Smith A, et al.
**摘要**：研究利用大肠杆菌系统成功表达并纯化重组VPRBP蛋白，证实其在体外通过调控CDK1磷酸化参与细胞周期停滞，为HIV-1 Vpr蛋白的作用机制提供分子基础。
2. **文献名称**：*"Structural analysis of VPRBP/DCAF1 reveals a substrate recognition module"*
**作者**：Zhang Y, et al.
**摘要**：通过X射线晶体学解析重组人源VPRBP的WD40结构域三维结构，揭示其与宿主蛋白UBR4的结合界面，阐明VPRBP作为E3泛素连接酶适配体的底物识别机制。
3. **文献名称**：*"VPRBP interacts with the CRISPR-Cas9 system to enhance gene editing efficiency"*
**作者**：Lee J, et al.
**摘要**：研究发现重组VPRBP蛋白可结合Cas9核酸酶，通过稳定其构象提升CRISPR基因编辑的靶向精度和效率，为优化基因治疗工具提供新策略。
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**注**：以上为模拟文献摘要，实际文献需通过PubMed、Web of Science等平台检索关键词(如VPRBP/DCAF1、recombinant protein、HIV Vpr interaction)获取。
VPRBP (Vascular Permeability Factor Receptor-Binding Protein), also known as RAMP2 (Receptor Activity-Modifying Protein 2), is a chaperone protein critical for regulating the activity of the calcitonin receptor-like receptor (CLR). Discovered in the early 2000s, it plays a pivotal role in modulating vascular and lymphatic functions by forming heterodimeric complexes with CLR. These complexes act as functional receptors for adrenomedullin (AM) and calcitonin gene-related peptide (CGRP), peptides involved in vasodilation, angiogenesis, and inflammation. VPRBP’s interaction with CLR ensures proper receptor trafficking, ligand specificity, and downstream signaling, impacting blood pressure homeostasis and vascular permeability.
Recombinant VPRBP protein is engineered using expression systems (e.g., E. coli, mammalian cells) to produce purified, bioactive forms for research and therapeutic applications. Its recombinant version retains the ability to bind CLR and influence receptor-ligand interactions, making it valuable for studying cardiovascular pathologies, sepsis, or tumor angiogenesis. Recent studies highlight its potential as a therapeutic target in conditions like preeclampsia, where disrupted adrenomedullin signaling contributes to vascular dysfunction. Additionally, recombinant VPRBP aids in structural studies to map binding domains and optimize peptide-based drugs targeting CLR-VPRBP complexes. Despite progress, challenges remain in understanding its tissue-specific regulation and post-translational modifications. Ongoing research focuses on leveraging recombinant VPRBP to develop novel biologics for cardiovascular and inflammatory diseases, underscoring its translational relevance in precision medicine.
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