| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TTPa |
| Uniprot No | P49638 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-278aa |
| 氨基酸序列 | MAEARSQPSAGPQLNALPDHSPLLQPGLAALRRRAREAGVPLAPLPLTDSFLLRFLRARDFDLDLAWRLLKNYYKWRAECPEISADLHPRSIIGLLKAGYHGVLRSRDPTGSKVLIYRIAHWDPKVFTAYDVFRVSLITSELIVQEVETQRNGIKAIFDLEGWQFSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFPDILPLEYGGEEFSMEDICQEWTNFIMKSEDYLSSISESIQ |
| 预测分子量 | 39.5 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TTP(血栓性血小板减少性紫癜)相关重组蛋白ADAMTS13的参考文献示例，内容基于真实研究领域，但文献标题和作者为模拟概括：
1. **"Recombinant ADAMTS13 Rescues Thrombotic Thrombocytopenic Purpura (TTP) in Murine Models"**
*作者：J. Evan Sadler 等*
摘要：研究重组ADAMTS13蛋白在小鼠TTP模型中的治疗作用，证明其能有效降解异常血小板微血栓，恢复血小板计数和器官功能。
2. **"Expression and Functional Characterization of Recombinant Human ADAMTS13 in CHO Cells"**
*作者：Masato Matsumoto 等*
摘要：描述利用中国仓鼠卵巢(CHO)细胞系统高效表达重组ADAMTS13.并验证其酶活性和结构稳定性，为临床生产奠定基础。
3. **"Phase I Clinical Trial of Recombinant ADAMTS13 in Congenital TTP Patients"**
*作者：Flora Peyvandi 等*
摘要：报道重组ADAMTS13在遗传性TTP患者中的首次人体试验，显示良好的耐受性、药代动力学特征及潜在疗效。
4. **"Mechanistic Insights into Recombinant ADAMTS13 Therapy for Acquired TTP"**
*作者：X. Long Zheng 等*
摘要：探讨重组ADAMTS13在获得性TTP(因自身抗体抑制ADAMTS13活性)中的治疗机制，包括剂量效应和免疫调控作用。
**注**：以上文献为领域内典型研究方向示例，实际引用需核对具体论文标题、作者及期刊信息。ADAMTS13重组蛋白研究多聚焦于生产优化、临床前/临床试验及机制解析。
**Background of TTPa Recombinant Protein**
Thrombotic thrombocytopenic purpura (TTP) is a rare, life-threatening disorder characterized by microvascular thrombosis, hemolytic anemia, and thrombocytopenia, often linked to severe deficiency of ADAMTS13. a metalloprotease that cleaves von Willebrand factor (vWF). In hereditary TTP, mutations in the *ADAMTS13* gene lead to enzyme dysfunction, while acquired TTP involves autoantibodies inhibiting ADAMTS13 activity. Traditional treatments include plasma exchange and immunosuppression, but these approaches have limitations, including incomplete efficacy and logistical challenges.
Recombinant ADAMTS13 (rADAMTS13), also referred to as TTPa recombinant protein, has emerged as a targeted therapeutic strategy. Produced via recombinant DNA technology in mammalian cell systems (e.g., CHO cells), this bioengineered protein mimics the natural enzyme’s structure and function, restoring vWF-cleaving activity to prevent pathogenic platelet aggregation. Preclinical and clinical studies demonstrate its potential to bypass the need for plasma-derived therapies, reduce relapse rates, and improve patient outcomes.
The development of rADAMTS13 addresses unmet needs in TTP management, particularly in congenital cases. Its design often incorporates modifications to enhance stability, reduce immunogenicity, and prolong circulation time. Recent trials highlight its efficacy in acute episodes and prophylactic use, with some formulations in advanced clinical phases. Challenges remain, such as optimizing production scalability and cost, but recombinant ADAMTS13 represents a paradigm shift toward precision medicine in thrombotic microangiopathies. Additionally, it complements emerging therapies like anti-vWF monoclonal antibodies (e.g., caplacizumab), offering a multifaceted approach to TTP treatment.
Overall, TTPa recombinant protein exemplifies advancements in biopharmaceuticals, leveraging molecular biology to target disease mechanisms at their root, with implications for both hereditary and autoimmune forms of TTP.
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