| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vWFCP |
| Uniprot No | Q76LX8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1328-1427aa |
| 氨基酸序列 | FINVAPHARIAIHALATNMGAGTEGANASYILIRDTHSLRTTAFHGQQVL YWESESSQAEMEFSEGFLKAQASLRGQYWTLQSWVPEMQDPQSWKGKEGT |
| 预测分子量 | 37 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vWFCP(ADAMTS13)重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容：
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1. **文献名称**: *Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura*
**作者**: Levy, G.G., et al.
**摘要**: 该研究首次克隆并鉴定了ADAMTS13基因，证明其在裂解vWF多聚体中的关键作用。通过重组表达ADAMTS13蛋白，证实其酶活性缺陷与遗传性血栓性血小板减少性紫癜(TTP)相关，为基因治疗和重组蛋白替代疗法奠定基础。
2. **文献名称**: *Recombinant ADAMTS13 normalizes von Willebrand factor cleavage activity in plasma of patients with acquired thrombotic thrombocytopenic purpura*
**作者**: Scully, M., et al.
**摘要**: 该临床试验评估了重组ADAMTS13蛋白在获得性TTP患者中的疗效。结果显示，输注重组蛋白可快速恢复血浆中vWF裂解活性，改善血小板计数及器官功能，且未出现严重不良反应，支持其作为TTP治疗的潜在方案。
3. **文献名称**: *Expression and characterization of recombinant human ADAMTS13 in mammalian cells*
**作者**: Plaimauer, B., et al.
**摘要**: 研究报道了在哺乳动物细胞(CHO细胞)中高效表达重组人ADAMTS13的方法。通过优化表达系统，获得高纯度及高活性的重组蛋白，其理化性质与天然蛋白一致，为大规模生产及临床应用提供了技术基础。
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以上文献涵盖了ADAMTS13重组蛋白的基因发现、临床前开发及治疗应用，均为该领域的关键研究。如需具体期刊信息或补充更多文献，可进一步检索PubMed或Web of Science数据库。
von Willebrand factor-cleaving protease (vWFCP), also known as ADAMTS13. is a plasma metalloprotease that regulates the multimeric size and activity of von Willebrand factor (VWF), a key glycoprotein in hemostasis. Discovered in the late 1990s, ADAMTS13 specifically cleaves ultra-large VWF multimers secreted from endothelial cells and platelets, preventing spontaneous platelet aggregation and microvascular thrombosis. Deficiencies in ADAMTS13 activity, either due to genetic mutations (congenital thrombotic thrombocytopenic purpura, or TTP) or autoimmune inhibitors (acquired TTP), result in uncontrolled VWF-platelet interactions, leading to life-threatening microangiopathic disorders.
Recombinant ADAMTS13 (rADAMTS13) has emerged as a targeted therapy for congenital TTP, addressing the unmet need for non-plasma-derived treatments. Produced using mammalian expression systems (e.g., Chinese hamster ovary cells), recombinant ADAMTS13 replicates the natural protease structure, including metalloprotease, disintegrin-like, and thrombospondin type-1 domains critical for substrate recognition and cleavage. Preclinical and clinical studies demonstrate its efficacy in restoring VWF processing, resolving thrombotic complications, and maintaining remission with prophylactic administration.
Research continues to optimize recombinant ADAMTS13’s pharmacokinetics, including half-life extension strategies like PEGylation or Fc fusion. Its development not only provides a precision medicine approach for hereditary TTP but also offers insights into broader applications for thrombotic disorders linked to VWF dysregulation. Current trials focus on dosing regimens and long-term safety, positioning recombinant ADAMTS13 as a transformative therapy in rare hematologic diseases.
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