| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vWA2 |
| Uniprot No | Q5GFL6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-755aa |
| 氨基酸序列 | LQEVHVS KETIGKISAA SKMMWCSAAV DIMFLLDGSN SVGKGSFERS KHFAITVCDG LDISPERVRV GAFQFSSTPH LEFPLDSFST QQEVKARIKR MVFKGGRTET ELALKYLLHR GLPGGRNASV PQILIIVTDG KSQGDVALPS KQLKERGVTV FAVGVRFPRW EELHALASEP RGQHVLLAEQ VEDATNGLFS TLSSSAICSS ATPDCRVEAH PCEHRTLEMV REFAGNAPCW RGSRRTLAVL AAHCPFYSWK RVFLTHPATC YRTTCPGPCD SQPCQNGGTC VPEGLDGYQC LCPLAFGGEA NCALKLSLEC RVDLLFLLDS SAGTTLDGFL RAKVFVKRFV RAVLSEDSRA RVGVATYSRE LLVAVPVGEY QDVPDLVWSL DGIPFRGGPT LTGSALRQAA ERGFGSATRT GQDRPRRVVV LLTESHSEDE VAGPARHARA RELLLLGVGS EAVRAELEEI TGSPKHVMVY SDPQDLFNQI PELQGKLCSR QRPGCRTQAL DLVFMLDTSA SVGPENFAQM QSFVRSCALQ FEVNPDVTQV GLVVYGSQVQ TAFGLDTKPT RAAMLRAISQ APYLGGVGSA GTALLHIYDK VMTVQRGARP GVPKAVVVLT GGRGAEDAAV PAQKLRNNGI SVLVVGVGPV LSEGLRRLAG PRDSLIHVAA YADLRYHQDV LIEWLCGEAK QPVNLCKPSP CMNEGSCVLQ NGSYRCKCRD GWEGPHCENR FLRRP |
| 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vWA2(von Willebrand factor A domain 2)重组蛋白的3条参考文献概述：
---
1. **文献名称**：*Recombinant vWA2 domain of collagen VI α3 chain promotes angiogenesis through integrin signaling*
**作者**：Smith J, et al.
**摘要内容**：研究证明重组表达的vWA2结构域可通过整合素α2β1受体激活下游FAK和MAPK信号通路，促进内皮细胞迁移和体外血管生成，提示其在组织修复中的潜在应用。
---
2. **文献名称**：*Structural and functional analysis of the vWA2 domain in extracellular matrix assembly*
**作者**：Lee H, et al.
**摘要内容**：通过X射线晶体学解析vWA2结构域的3D构象，发现其通过金属离子依赖的界面与层粘连蛋白相互作用，调控细胞外基质的稳定性，为病理状态下的基质重塑机制提供依据。
---
3. **文献名称**：*vWA2 recombinant protein inhibits tumor metastasis by blocking cell-matrix adhesion*
**作者**：Wang Q, et al.
**摘要内容**：体外实验表明，重组vWA2蛋白可竞争性抑制肿瘤细胞与胶原基质的黏附，降低侵袭能力，并通过小鼠模型验证其对肺转移的抑制作用，提示其作为抗转移治疗分子的潜力。
---
注：以上文献为虚拟示例，实际研究中请通过PubMed或Web of Science检索具体论文。
**Background of vWA2 Recombinant Protein**
The von Willebrand factor type A (vWA) domain is a conserved structural motif found in proteins involved in diverse cellular processes, including cell adhesion, migration, and extracellular matrix interactions. The vWA2 recombinant protein refers to a engineered version of a protein containing the second vWA domain, often derived from parent proteins such as integrins, collagens, or other extracellular matrix-associated molecules. This domain typically mediates protein-protein or protein-ligand interactions through metal ion-dependent adhesion sites (MIDAS), enabling critical roles in signaling pathways and tissue homeostasis.
Recombinant vWA2 proteins are produced via heterologous expression systems (e.g., *E. coli*, mammalian cells) to ensure high purity and functionality. Their design often includes tags (e.g., His-tag, GST) for simplified purification and detection. Researchers utilize these proteins to study molecular interactions, particularly in contexts like inflammation, cancer metastasis, or wound healing, where vWA domain-mediated adhesion is pivotal. For example, vWA2 domains in integrins facilitate cell binding to ligands such as fibronectin, influencing cell behavior and tissue remodeling.
Additionally, vWA2 recombinant proteins serve as tools for structural biology (e.g., crystallography) to resolve interaction mechanisms or for developing therapeutic agents targeting adhesion-related diseases. Their role in modulating immune responses or angiogenesis has also spurred interest in drug discovery. Overall, vWA2 recombinant proteins provide a versatile platform for deciphering extracellular signaling networks and advancing biomedical applications.
×
