| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VWC2 |
| Uniprot No | Q2TAL6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-325aa |
| 氨基酸序列 | MPSSTAMAVG ALSSSLLVTC CLMVALCSPS IPLEKLAQAP EQPGQEKREH ASRDGPGRVN ELGRPARDEG GSGRDWKSKS GRGLAGREPW SKLKQAWVSQ GGGAKAGDLQ VRPRGDTPQA EALAAAAQDA IGPELAPTPE PPEEYVYPDY RGKGCVDESG FVYAIGEKFA PGPSACPCLC TEEGPLCAQP ECPRLHPRCI HVDTSQCCPQ CKERKNYCEF RGKTYQTLEE FVVSPCERCR CEANGEVLCT VSACPQTECV DPVYEPDQCC PICKNGPNCF AETAVIPAGR EVKTDECTIC HCTYEEGTWR IERQAMCTRH ECRQM |
| 预测分子量 | 34 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3篇涉及VWC2重组蛋白的相关文献摘要概述(注：文献为虚拟示例，实际需通过学术数据库检索验证)：
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1. **文献名称**: *"Recombinant VWC2 domain modulates TGF-β signaling in vitro"*
**作者**: Zhang Y. et al.
**摘要**: 本研究通过在大肠杆菌系统中表达并纯化重组人VWC2结构域蛋白，发现其可特异性结合TGF-β1.抑制SMAD信号通路激活，提示VWC2可能在细胞外基质调控生长因子信号中起重要作用。
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2. **文献名称**: *"Expression and functional characterization of VWC2 in cancer cell adhesion"*
**作者**: Lee S. et al.
**摘要**: 利用哺乳动物细胞表达系统制备重组VWC2蛋白，证明其通过整合素αvβ3介导抑制肿瘤细胞迁移，为VWC2在癌症转移中的潜在治疗价值提供实验依据。
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3. **文献名称**: *"Structural analysis of the VWC2 domain from collagen VI using recombinant protein"*
**作者**: Müller R. et al.
**摘要**: 通过昆虫细胞表达系统获得高纯度VWC2重组蛋白，结合X射线晶体学解析其三维结构，揭示了该结构域与胶原蛋白相互作用的关键氨基酸残基。
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**提示**：实际文献需在PubMed、Web of Science等平台以关键词“VWC2 recombinant”“VWC2 domain expression”检索，建议结合具体研究领域(如细胞信号、疾病机制)筛选近期论文。
VWC2 (Von Willebrand Factor C domain-containing protein 2) is a member of the VWC protein family, characterized by the presence of Von Willebrand Factor type C (VWC) domains. These domains are evolutionarily conserved structural motifs involved in protein-protein interactions, extracellular matrix organization, and cellular signaling. VWC2. also known as collagen and calcium-binding EGF domain-containing protein 1 (CCBE1) in certain contexts, has gained attention for its critical role in developmental biology, particularly in lymphatic system formation. Studies show it regulates lymphangiogenesis by activating VEGF-C signaling, essential for embryonic vascular and lymphatic development.
Recombinant VWC2 protein is engineered using biotechnological platforms (e.g., bacterial, mammalian, or insect cell systems) to produce purified, functional VWC2 for research and therapeutic applications. Its recombinant form enables precise study of molecular mechanisms, such as interactions with proteases (e.g., ADAMTS3) to process pro-VEGF-C into mature growth factors. Dysregulation of VWC2 is linked to human diseases, including hereditary lymphedema and cancer metastasis, underscoring its biomedical relevance.
In drug discovery, recombinant VWC2 serves as a tool to explore pathways in lymphatic disorders or tumor microenvironment modulation. Its potential as a therapeutic agent or biomarker is under investigation, particularly for conditions involving impaired lymphatic drainage or aberrant angiogenesis. Current research also focuses on optimizing recombinant production to ensure proper post-translational modifications, which are vital for functional activity. Overall, VWC2 exemplifies how structural domains dictate biological function and highlights the utility of recombinant proteins in bridging basic science with clinical innovation.
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