| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vWA3A |
| Uniprot No | A6NCI4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1184aa |
| 氨基酸序列 | MKKYRKISIGCFAMATQTSHVFHGQENMFLENHCIRRNTGRDSKKPLKQKNMNGLGQNSDNGLLVTHVNQTQDLLRLQGSETQSSDWEDSEDWLSAHSLKCQKLTLADLISQGTEVLEEGTNVVQKICFSTQIIRHFESKLSDTIEVYQERIQWLTENSKKAFGLIKGARVSILIDVSAISSGPQKEEFQKDLMSLIDEQLSHKEKLFVLSFGTNAGSLWPDPMEVSASTLQELKLWVKTLQPDGGSNLLQALKKIFTLKGLDSLVAIMRSCPDQPSEILSDYIQQSTMGRDLIIHFITYRCDDQMPPAVLKNLAEAVRGYYHCYSPKMEHYTSRDMDELLAEIQKAQSLLSHVQALQHSSPCEALTCTMEEISTEITNGPLISLLPKPPKHDAPLTIEFPNLDKTSAEWLKVNGLKAKKLSLYQVLAPNAFSPVEEFVPILQKTVSSTIHEKAMIQFEWHDGTVKNIHVDPPFLYKYQQQLSRAMRMYERRIEWLSLASRRIWGTVCEKRVVVLLDISATNSMYIIHIQHSLRLLLEEQLSNKDCFNLIAFGSTIESWRPEMVPVSHNNLQSAWRWALNLRCRGSRNVLSALRKAVEVDFKDKDKHQSQGIYLFTGGIPDQDMPTLSAYMAEACGGCDLQLNVCLFYVGEPKMDTTPPARYASHTDTAAAYKEVTRAAGGRFHWFGDTGIYESDDINSIMSEMEKALNYSQKCAFLMASLKNHSGKVLGSSALPKEKPKTLQLRSQPKKLCPPRPTVPLGARMSIKDDPDREKSPPLKSLKWRPLSSRVGISPAAAQPTKEGMMELRRKTKSREAETSLLLFYTEKGNDVGSVYKKYPQGRGLRRTSSSIDLPRKDTVCSSQEWVAKYGLKKLKLEISRCMGPNCTHQKSGQRSASAKHCSIFPSVEIHGVVRHIQWTPREMEVYIRHLEKVLRRYVQRLQWLLSGSRRLFGTVLESKVCILLDTSGSMGPYLQQVKTELVLLIWEQLRKCCDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQGSTSILQALLKAFSFHDLEGLYLLTDGKPDTSCSLVLNEVQKLREKRDVKVHTISLNCSDRAAVEFLRKLASFTGGRYHCPVGEDTLSKIHSLLTKGFINEKDPTLPPFEGDDLRILAQEITKARSFLWQAQSFRSQLQKKNDAEPKVTLS |
| 预测分子量 | 134 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. |
以下为模拟生成的关于vWA3A重组蛋白的参考文献示例(非真实文献，仅供格式参考)：
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1. **《Functional characterization of recombinant vWA3A domain in collagen-binding activity》**
*Zhang, L. et al. (2021)*
摘要：本研究在大肠杆菌中成功表达并纯化了vWA3A重组蛋白，通过表面等离子共振技术证实其与IV型胶原的高亲和力结合，揭示了该结构域在细胞外基质相互作用中的关键作用。
2. **《Structural insights into vWA3A-mediated cell adhesion signaling》**
*Wang, Y. & Tanaka, K. (2019)*
摘要：利用X射线晶体学解析vWA3A重组蛋白的3D结构(分辨率2.1Å)，结合突变实验验证了其金属离子依赖性整合素结合位点，为开发靶向细胞迁移的抑制剂提供理论依据。
3. **《Recombinant vWA3A as a potential biomarker in autoimmune disorders》**
*Gupta, R. et al. (2020)*
摘要：通过昆虫细胞系统表达vWA3A重组蛋白，临床样本ELISA检测显示其在类风湿性关节炎患者血清中显著高表达，提示其作为自身免疫疾病生物标志物的潜力。
4. **《Optimization of vWA3A recombinant protein production in mammalian expression systems》**
*Chen, S. et al. (2022)*
摘要：比较CHO细胞和HEK293系统中的vWA3A重组蛋白产量及糖基化修饰差异，开发出高稳定性的纯化工艺，为后续抗体药物开发奠定基础。
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**备注**：以上文献为模拟生成内容，实际文献建议通过PubMed、Web of Science或Google Scholar等平台检索关键词如“vWA3A recombinant protein”“von Willebrand factor A domain 3A”等获取。真实研究多聚焦于该结构域在细胞黏附、疾病机制或蛋白工程中的应用。
vWA3A recombinant protein is a engineered protein construct derived from the von Willebrand Factor A (vWA) domain, a conserved structural motif involved in cell adhesion, extracellular matrix interactions, and signaling. The "vWA3A" designation typically refers to the third A-domain (A3) of the von Willebrand Factor (VWF), a key component in hemostasis that mediates platelet binding to collagen at injury sites. This domain plays a critical role in maintaining structural integrity and ligand-binding specificity.
Recombinant vWA3A is produced using heterologous expression systems (e.g., E. coli, mammalian cells) to ensure proper folding of its globular α/β structure. Its production enables detailed studies of VWF-related pathologies, such as von Willebrand disease or thrombotic disorders, by providing a purified, functional domain for biochemical assays. Researchers also leverage vWA3A to investigate collagen-binding mechanisms, platelet adhesion dynamics, and molecular interactions with heparin or other extracellular matrix components.
Beyond hematology, vWA3A has applications in tissue engineering and biomaterial design due to its adhesive properties. Structural studies using recombinant vWA3A have revealed conformational changes during ligand binding, informing drug development for coagulation disorders. Recent interest extends to cancer research, as VWF domains may influence tumor metastasis through cell-matrix interactions. The recombinant format allows site-specific mutagenesis to dissect functional residues, making it a versatile tool for both basic research and therapeutic target validation.
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