纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MMP15 |
Uniprot No | P51511 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-669aa |
氨基酸序列 | MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATERPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGDFGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLYCKRSLQEWV |
预测分子量 | 75,8 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MMP15重组蛋白的3篇参考文献概览:
1. **文献名称**:*"Recombinant expression and characterization of human matrix metalloproteinase-15 (MMP-15) in mammalian cells"*
**作者**:Smith A, et al.
**摘要**:研究报道了人源MMP15在HEK293细胞中的重组表达及纯化方法,分析了其酶活性及在细胞外基质降解中的作用,证实其与肿瘤侵袭的相关性。
2. **文献名称**:*"Structural insights into the catalytic domain of membrane-type matrix metalloproteinase-15 (MT2-MMP)"*
**作者**:Lee JH, et al.
**摘要**:通过重组表达MT2-MMP(MMP15)的催化结构域,解析其晶体结构,揭示了底物结合位点的特征,为靶向抑制剂设计提供了依据。
3. **文献名称**:*"Functional analysis of recombinant MMP-15 in endothelial cell migration and angiogenesis"*
**作者**:Garcia-Castro M, et al.
**摘要**:利用大肠杆菌表达系统制备重组MMP15蛋白,发现其促进血管内皮细胞迁移和血管生成,提示其在组织修复和病理微环境中的潜在作用。
*注:以上文献信息为示例性质,实际引用时需核实具体来源。*
**Background of MMP15 Recombinant Protein**
Matrix metalloproteinase 15 (MMP15), also known as membrane-type 3 MMP (MT3-MMP), is a member of the zinc-dependent endopeptidase family involved in extracellular matrix (ECM) remodeling. As a membrane-anchored protease, MMP15 plays critical roles in physiological processes such as tissue development, wound healing, and angiogenesis, as well as pathological conditions including cancer progression, inflammation, and fibrosis. Unlike soluble MMPs, MMP15 contains a transmembrane domain, enabling its direct interaction with cell surface substrates and localized proteolytic activity.
Structurally, MMP15 consists of a pro-domain, catalytic domain, hinge region, and hemopexin-like domain. Its activation requires cleavage of the inhibitory pro-domain, releasing the catalytically active enzyme. MMP15 not only degrades ECM components (e.g., fibronectin, laminin) but also processes cytokines, growth factors, and other MMPs (e.g., pro-MMP2), amplifying proteolytic cascades. In cancer, MMP15 promotes tumor invasion, metastasis, and angiogenesis by facilitating ECM breakdown and releasing growth factors like VEGF. Its dysregulation is linked to poor prognosis in various cancers, including breast, colorectal, and glioblastoma.
Recombinant MMP15 protein is produced using expression systems (e.g., mammalian, insect cells) to ensure proper post-translational modifications and enzymatic activity. It is purified via affinity chromatography and validated for functionality using substrates like fluorogenic peptides or gelatin zymography. Researchers utilize recombinant MMP15 to study its biological roles, screen inhibitors for therapeutic development, and model ECM-related diseases.
Despite its significance, MMP15's unique substrate profile and regulatory mechanisms remain understudied compared to other MMPs, making it a compelling target for further research in both basic and applied biomedical sciences.
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