| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MEP1a |
| Uniprot No | Q16819 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-601aa |
| 氨基酸序列 | ADPVPIKYLPEENVHDADFGEQKDISEINLAAGLDLFQGDILLQKSRNGL RDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESS YIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQS RTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFS FNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNCTTTHTLLDH CTFEKANICGMIQGTRDDTDWAHQDSAQAGEVDHTLLGQCTGAGYFMQFS TSSGSAEEAALLESRILYPKRKQQCLQFFYKMTGSPSDRLVVWVRRDDST GNVRKLVKVQTFQGDDDHNWKIAHVVLKEEQKFRYLFQGTKGDPQNSTGG IYLDDITLTETPCPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFG VTLYPNSRESSGYLRLAFHVCSGENDAILEWPVENRQVIITILDQEPDVR NRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWS GFISHQMLKRRSFLKNDDLIIFVDFEDITHLSQHHHHHH |
| 预测分子量 | 67 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MEP1α(Meprin A)重组蛋白的假设性参考文献示例(实际文献需根据数据库核实)：
1. **文献名称**: *"Recombinant expression and functional characterization of Meprin α subunit (MEP1A) in human kidney cells"*
**作者**: Bond JS, et al.
**摘要**: 研究通过哺乳动物表达系统成功重组表达了人源MEP1A蛋白，证实其在体外能降解IV型胶原蛋白，并揭示其酶活性依赖锌离子，为肾脏疾病中基底膜重塑机制提供依据。
2. **文献名称**: *"Structural insights into MEP1A protease: Crystallographic analysis of the recombinant protein"*
**作者**: Kaushal GP, et al.
**摘要**: 首次解析了重组MEP1A的晶体结构，明确了其金属蛋白酶结构域的关键催化位点，为设计特异性抑制剂治疗炎症性肠病奠定基础。
3. **文献名称**: *"Role of recombinant MEP1A in TGF-β1 activation during fibrosis"*
**作者**: Jefferson T, et al.
**摘要**: 实验表明重组MEP1A可通过切割潜伏态TGF-β1前体，释放活性因子促进成纤维细胞活化，提示其在器官纤维化中的潜在病理作用。
4. **文献名称**: *"Development of a high-yield E. coli system for recombinant MEP1A production"*
**作者**: Smith C, Beynon RJ
**摘要**: 优化大肠杆菌表达体系实现MEP1A可溶性高效表达，通过亲和层析纯化获得高纯度蛋白，为大规模研究其酶学特性提供可靠方法。
注：以上内容为模拟示例，实际文献需通过PubMed/Google Scholar检索确认。
**Background of MEP1A Recombinant Protein**
Meprin 1A (MEP1A), a member of the astacin family of metalloproteases, is a multidomain, zinc-dependent protease involved in extracellular matrix (ECM) remodeling, inflammation, and tissue homeostasis. It is expressed as a type I transmembrane protein or secreted glycoprotein, depending on alternative splicing and post-translational processing. Structurally, MEP1A consists of a pro-domain, a catalytic domain with a conserved zinc-binding motif, a MAM domain (mediating protein-protein interactions), a TRAF domain, and an EGF-like domain. Its enzymatic activity is regulated by proteolytic cleavage of the pro-domain and interactions with endogenous inhibitors like fetuin-A.
MEP1A is primarily expressed in epithelial cells, particularly in the kidney, intestine, and skin. It cleaves diverse substrates, including ECM components (collagen, laminin), cytokines (IL-1β, IL-18), and growth factors, influencing cell adhesion, migration, and immune responses. Dysregulation of MEP1A is linked to pathologies such as renal fibrosis, inflammatory bowel disease (IBD), and cancer. For example, in colorectal cancer, elevated MEP1A levels correlate with tumor progression and metastasis, likely via ECM degradation and activation of pro-tumorigenic signaling pathways.
Recombinant MEP1A proteins are produced using expression systems (e.g., mammalian or insect cells) to ensure proper folding and post-translational modifications. These proteins serve as critical tools for studying substrate specificity, enzymatic kinetics, and inhibitor screening. They also aid in developing therapeutic strategies targeting MEP1A-associated diseases. Recent studies highlight its dual role as both a tissue repair promoter and a pathological mediator, underscoring the need for context-specific therapeutic approaches. Research continues to explore its regulatory mechanisms and potential as a diagnostic or prognostic biomarker.
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