| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VWA5B2 |
| Uniprot No | Q8N398 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 781-862aa |
| 氨基酸序列 | PRKPSLGAILDGPSPEPGQQLGQGLDDSGNLLSPAPMDWDMLMEPPFLFTAVPPSGELAPPAVPPQAPRCHVVIRGLCGEQP |
| 预测分子量 | 24.6 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VWA5B2重组蛋白的3篇参考文献的简要整理(注：VWA5B2相关研究较少，以下内容为基于领域知识的模拟示例)：
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1. **文献名称**: "Recombinant expression and functional analysis of VWA5B2 in extracellular matrix remodeling"
**作者**: Li et al., 2021
**摘要**: 本研究首次在大肠杆菌中成功表达并纯化了重组VWA5B2蛋白，发现其通过结合胶原蛋白调控细胞黏附，提示其在组织修复中的潜在作用。
2. **文献名称**: "VWA5B2 interacts with integrin α3β1 and modulates cancer cell migration"
**作者**: Smith & Johnson, 2019
**摘要**: 通过哺乳动物细胞系统重组表达VWA5B2.发现其与整合素α3β1相互作用，抑制肿瘤细胞的迁移能力，为癌症治疗提供新靶点。
3. **文献名称**: "Structural characterization of the VWA5B2 domain and its role in immune regulation"
**作者**: Wang et al., 2020
**摘要**: 利用昆虫细胞表达系统获得高纯度VWA5B2蛋白，解析其晶体结构，揭示其通过调控TGF-β信号通路参与免疫稳态的分子机制。
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**注意**：上述文献为虚构示例，实际研究中关于VWA5B2的公开数据有限。建议通过PubMed或Google Scholar以**"VWA5B2 recombinant"**或**"VWA5B2 function"**为关键词检索最新文献，或关注其所属的VWA蛋白家族(如VWA5A等)相关研究。
**Background of VWA5B2 Recombinant Protein**
The VWA5B2 (Von Willebrand Factor A Domain Containing Protein 5B2) recombinant protein is a engineered version of a naturally occurring protein encoded by the *VWA5B2* gene in humans. This protein belongs to the von Willebrand factor A (VWA) domain-containing family, characterized by the presence of a conserved VWA domain—a structural motif involved in protein-protein interactions, cell adhesion, and extracellular matrix (ECM) organization. The VWA domain often contains a metal ion-dependent adhesion site (MIDAS), which facilitates binding to ligands like integrins or collagen, suggesting roles in cellular signaling and tissue homeostasis.
While the precise biological function of VWA5B2 remains under investigation, studies suggest its potential involvement in cellular adhesion, tissue development, or immune regulation. Dysregulation of VWA domain-containing proteins has been linked to diseases such as cancer, fibrosis, and autoimmune disorders, positioning VWA5B2 as a candidate for exploring disease mechanisms.
Recombinant VWA5B2 is typically produced using heterologous expression systems (e.g., *E. coli*, mammalian cells) to ensure high purity and functionality. Its production enables researchers to study protein structure, interactions, and signaling pathways in vitro or in vivo. Applications include elucidating its role in ECM remodeling, validating binding partners via assays like ELISA or pull-down experiments, and screening for therapeutic agents targeting VWA5B2-associated pathways. Additionally, recombinant VWA5B2 may serve as an antigen for antibody development or a tool for diagnostic research.
Despite its emerging significance, further studies are needed to fully characterize VWA5B2's physiological roles and therapeutic potential, highlighting its importance in both basic and translational biomedical research.
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