| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADAMTS10 |
| Uniprot No | Q9H324 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1103aa |
| 氨基酸序列 | MAPACQILRWALALGLGLMFEVTHAFRSQDEFLSSLESYEIAFPTRVDHNGALLAFSPPPPRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAARPHCLYAGHLQGQASTSHVAISTCGGLHGLIVADEEEYLIEPLHGGPKGSRSPEESGPHVVYKRSSLRHPHLDTACGVRDEKPWKGRPWWLRTLKPPPARPLGNETERGQPGLKRSVSRERYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVNHSGHGNAIPENGVANHDTAVLITRYDICIYKNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTFGMNHDGVGNSCGARGQDPAKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLNNRPPRQDFVYPTVAPGQAYDADEQCRFQHGVKSRQCKYGEVCSELWCLSKSNRCITNSIPAAEGTLCQTHTIDKGWCYKRVCVPFGSRPEGVDGAWGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCPPGSQDFREVQCSEFDSIPFRGKFYKWKTYRGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPDTVDICVSGECKHVGCDRVLGSDLREDKCRVCGGDGSACETIEGVFSPASPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGTPQPHRLPLAGTTFQLRQGPDQVQSLEALGPINASLIVMVLARTELPALRYRFNAPIARDSLPPYSWHYAPWTKCSAQCAGGSQVQAVECRNQLDSSAVAPHYCSAHSKLPKRQRACNTEPCPPDWVVGNWSLCSRSCDAGVRSRSVVCQRRVSAAEEKALDDSACPQPRPPVLEACHGPTCPPEWAALDWSECTPSCGPGLRHRVVLCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPARWVAGEWGECSAQCGVGQRQRSVRCTSHTGQASHECTEALRPPTTQQCEAKCDSPTPGDGPEECKDVNKVAYCPLVLKFQFCSRAYFRQMCCKTCHGH |
| 预测分子量 | 120,8 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ADAMTS10重组蛋白的3篇参考文献示例(内容基于模拟学术文献整理，供参考)：
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1. **文献名称**：*ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome*
**作者**：Dagoneau N, et al.
**摘要**：本研究首次克隆并表达了人源ADAMTS10重组蛋白，发现其在细胞外基质组装中起关键作用。通过功能实验表明，ADAMTS10突变导致韦尔-马切萨尼综合征患者的纤维连接蛋白代谢异常。
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2. **文献名称**：*Recombinant ADAMTS10 binds fibrillin-1 and regulates microfibril assembly*
**作者**：Kutz WE, et al.
**摘要**：利用哺乳动物细胞系统表达ADAMTS10重组蛋白，证实其通过结合原纤维蛋白-1(fibrillin-1)调控微纤维的形成。研究揭示了ADAMTS10在维持结缔组织稳态中的分子机制。
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3. **文献名称**：*Functional characterization of ADAMTS10 protease activity using a recombinant C-terminal fragment*
**作者**：Enomoto H, et al.
**摘要**：通过构建ADAMTS10羧基端重组蛋白片段，分析其蛋白酶活性及底物特异性，发现其对弹性蛋白前体具有切割能力，提示其在组织发育和疾病中的潜在作用。
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注：以上文献信息为示例性质，实际研究中请通过学术数据库(如PubMed、Web of Science)检索最新及具体文献。
ADAMTS10 (A Disintegrin and Metalloproteinase with Thrombospondin Motifs 10) is a secreted extracellular matrix (ECM)-associated protease belonging to the ADAMTS family, which plays critical roles in tissue development, remodeling, and homeostasis. It is characterized by a conserved modular structure, including a prodomain, metalloproteinase domain, disintegrin-like module, thrombospondin type-1 (TSP1) repeats, and a unique C-terminal domain. Unlike many ADAMTS proteases, ADAMTS10 lacks canonical proteolytic activity against common ECM substrates like aggrecan or versican, suggesting non-enzymatic or substrate-specific regulatory functions.
Genetic studies link ADAMTS10 mutations to Weill-Marchesani syndrome (WMS), a rare connective tissue disorder marked by short stature, brachydactyly, lens dislocation, and cardiovascular abnormalities. ADAMTS10 is essential for microfibril assembly, particularly in elastic fibers and zonular filaments of the eye, interacting with fibrillin-1 to regulate ECM organization. Its dysfunction disrupts microfibril integrity, impairing tissue elasticity and growth factor signaling (e.g., TGF-β).
Recombinant ADAMTS10 protein is produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation and proteolytic processing. This engineered protein serves as a tool to study ADAMTS10’s structure-function relationships, ECM interactions, and pathogenic mechanisms in WMS. It also has therapeutic potential, including enzyme replacement strategies or modulating microfibril defects in genetic disorders. Challenges in its application include low natural abundance, complex purification due to multiple domains, and limited understanding of its precise molecular targets. Ongoing research aims to elucidate its role in developmental pathways and explore translational opportunities for connective tissue diseases.
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