| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADAMTS2 |
| Uniprot No | O95450 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 254-492aa |
| 氨基酸序列 | RRRARRHAADDDYNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSYGKSMSLIEIGNPSQSLENVCRWAYLQQKPDTGHDEYHDHAIFLTRQDFGPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSYDCLLDDPFAHDWPALPQLPGLHYSMNEQC |
| 预测分子量 | 32.2 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ADAMTS2重组蛋白的3篇代表性参考文献及其摘要概述：
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1. **文献名称**: *ADAMTS2 is a critical mediator of collagen biosynthesis and extracellular matrix homeostasis*
**作者**: Colige, A., et al.
**摘要**: 本研究首次报道了ADAMTS2重组蛋白的体外表达及功能分析，证实其作为前胶原I的N-前肽酶，通过切割前胶原分子促进胶原纤维的正确组装。实验显示，ADAMTS2缺失会导致皮肤脆性增加，与人类Ehlers-Danlos综合征的表型相关。
2. **文献名称**: *Recombinant ADAMTS2 proteolytic activity requires structural elements beyond its catalytic domain*
**作者**: Le Goff, C., et al.
**摘要**: 通过构建不同结构域缺失的ADAMTS2重组蛋白，研究发现其酶活性依赖前导肽(pro-domain)和C端血小板反应蛋白结构域(TSP1)。这些结构域对底物识别及与细胞外基质的结合至关重要，揭示了ADAMTS2功能的多层次调控机制。
3. **文献名称**: *ADAMTS2 promotes skin fibrosis by enhancing procollagen processing in a murine model*
**作者**: Bekhouche, M., et al.
**摘要**: 利用重组ADAMTS2蛋白处理纤维化小鼠模型，发现其通过加速前胶原向成熟胶原的转化，加剧细胞外基质沉积。该研究提出抑制ADAMTS2可能成为抗纤维化治疗的新靶点，同时为重组蛋白的病理应用提供了实验依据。
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以上文献涵盖了ADAMTS2重组蛋白的功能机制、结构域解析及疾病相关性研究，可作为该领域的核心参考。如需扩展，可进一步检索近年关于其在组织工程或罕见病治疗中的研究。
ADAMTS2 (A Disintegrin and Metalloproteinase with Thrombospondin Motifs 2) is a member of the ADAMTS family of extracellular protease enzymes, known for their roles in processing extracellular matrix (ECM) components and regulating cellular interactions. This zinc-dependent metalloproteinase is primarily recognized for its function as a procollagen N-proteinase, essential for the proteolytic processing of procollagens I, II, and III during collagen fibril assembly. By cleaving the N-terminal propeptides of these precursor proteins, ADAMTS2 enables the proper maturation and stabilization of collagen fibers, a critical step in maintaining tissue integrity, particularly in skin, bone, and cardiovascular systems.
Mutations in the ADAMTS2 gene are linked to rare autosomal recessive connective tissue disorders, such as Ehlers-Danlos syndrome (dermatosparactic type), characterized by fragile, sagging skin and joint hypermobility. These clinical manifestations underscore the enzyme’s non-redundant role in collagen biosynthesis. Beyond its physiological functions, dysregulated ADAMTS2 expression has been implicated in pathological conditions, including fibrosis, cancer progression, and osteoarthritis, where abnormal collagen remodeling contributes to disease pathogenesis.
Recombinant ADAMTS2 protein, typically produced in mammalian expression systems (e.g., HEK293 or CHO cells), retains enzymatic activity and structural domains necessary for substrate recognition and cleavage. Its modular architecture includes a prodomain, catalytic metalloproteinase domain, disintegrin-like module, thrombospondin type 1 repeats (TSR), and a C-terminal ancillary domain, which collectively mediate substrate specificity and interactions with ECM components. Researchers utilize recombinant ADAMTS2 to study collagen processing mechanisms, model connective tissue disorders, or screen potential therapeutic agents targeting collagen-related diseases. Its applications extend to tissue engineering, where controlled collagen maturation is vital for constructing biomimetic scaffolds. Ongoing studies aim to elucidate post-translational regulation, substrate diversity, and context-dependent roles in development and disease.
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