| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP10 |
| Uniprot No | P09238 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 99-476aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSFSSFPGMPKWRKTHLTYRIVNYTPDLP RDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDG PGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHELGHSLGL FHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYGPPPASTEEPLVP TKSVPSGSEMPAKCDPALSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEF HLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGNEVQAGYPRGI HTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLI ADDFPGVEPKVDAVLQAFGFFYFFSGSSQFEFDPNARMVTHILKSNSWLH C |
| 预测分子量 | 45 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3篇与MMP10重组蛋白相关的模拟参考文献(注：内容为模拟生成，非真实文献)：
1. **"Recombinant MMP10 promotes epithelial-mesenchymal transition in colorectal cancer cells"**
- **作者**: Smith A, et al.
- **摘要**: 研究通过大肠杆菌表达系统纯化重组MMP10蛋白，发现其通过激活TGF-β信号通路增强肿瘤细胞侵袭和转移能力，提示MMP10在结直肠癌进展中的潜在作用。
2. **"Functional characterization of recombinant MMP10 in extracellular matrix remodeling"**
- **作者**: Lee JH, Kim T.
- **摘要**: 利用哺乳动物细胞表达的重组MMP10蛋白，验证其对胶原蛋白IV和层粘连蛋白的降解活性，揭示其在组织修复和纤维化疾病中的双重调控机制。
3. **"Development of a high-yield MMP10 recombinant protein production system using insect cells"**
- **作者**: Gonzalez R, et al.
- **摘要**: 报道基于杆状病毒-昆虫细胞系统的高效MMP10重组蛋白表达策略，优化纯化流程并验证其酶活性，为大规模制备提供技术参考。
4. **"MMP10 as a biomarker in chronic inflammation: Insights from recombinant protein-based assays"**
- **作者**: Wang Y, et al.
- **摘要**: 通过重组MMP10蛋白建立ELISA检测方法，发现其在慢性炎症患者血清中显著上调，提示其作为炎症性疾病诊断标志物的潜力。
**注**：以上内容为示例性质，实际文献需通过PubMed或Web of Science等平台检索关键词(如"MMP10 recombinant protein")。近年研究多聚焦于MMP10在癌症、纤维化及再生医学中的机制与应用。
Matrix metalloproteinase 10 (MMP10), also known as stromelysin-2. is a member of the zinc-dependent endopeptidase family involved in extracellular matrix (ECM) remodeling. Encoded by the MMP10 gene in humans, this protease shares structural homology with other MMPs, featuring a prodomain, catalytic domain, and hemopexin-like domain. MMP10 is synthesized as an inactive zymogen (pro-MMP10) that requires proteolytic cleavage for activation. It primarily degrades ECM components such as collagen type IV, gelatin, fibronectin, and proteoglycans, but exhibits narrower substrate specificity compared to broader-spectrum MMPs like MMP3 or MMP9.
Biologically, MMP10 plays dual roles in tissue homeostasis and disease. It contributes to wound healing, embryonic development, and immune regulation by modulating cell-matrix interactions and releasing growth factors. However, dysregulated MMP10 expression is implicated in pathological conditions including chronic inflammation, fibrosis, arthritis, and cancer progression. In tumors, MMP10 facilitates angiogenesis, invasion, and metastasis by processing ECM barriers and activating signaling pathways.
Recombinant MMP10 proteins are engineered for research and therapeutic applications. Produced typically in mammalian or insect expression systems to ensure proper post-translational modifications (e.g., glycosylation), they are purified via affinity chromatography. The recombinant form often includes tags (e.g., His-tag) for detection and purification. Researchers utilize these proteins to study protease-substrate interactions, screen MMP inhibitors, and model ECM remodeling processes. Notably, recombinant MMP10 requires activation (e.g., by APMA or trypsin) to remove the inhibitory prodomain before functional assays. Its activity is frequently validated using fluorogenic substrates or gelatin zymography.
As MMP10 emerges as a potential biomarker and therapeutic target, recombinant variants remain crucial tools for dissecting its pathophysiological mechanisms and developing targeted therapies.
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