| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP17 |
| Uniprot No | Q9ULZ9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 126-565aa |
| 氨基酸序列 | QAPAP TKWNKRNLSW RVRTFPRDSP LGHDTVRALM YYALKVWSDI APLNFHEVAG SAADIQIDFS KADHNDGYPF DGPGGTVAHA FFPGHHHTAG DTHFDDDEAW TFRSSDAHGM DLFAVAVHEF GHAIGLSHVA AAHSIMRPYY QGPVGDPLRY GLPYEDKVRV WQLYGVRESV SPTAQPEEPP LLPEPPDNRS SAPPRKDVPH RCSTHFDAVA QIRGEAFFFK GKYFWRLTRD RHLVSLQPAQ MHRFWRGLPL HLDSVDAVYE RTSDHKIVFF KGDRYWVFKD NNVEEGYPRP VSDFSLPPGG IDAAFSWAHN DRTYFFKDQL YWRYDDHTRH MDPGYPAQSP LWRGVPSTLD DAMRWSDGAS YFFRGQEYWK VLDGELEVAP GYPQSTARDW LVCGDSQADG SVAAGVDAAE GPRAPPGQHD QSRSEDGYEV CSCTS |
| 预测分子量 | 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MMP17重组蛋白的3篇代表性文献摘要概览：
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1. **文献名称**：*"Expression and characterization of recombinant matrix metalloproteinase-17 (MMP-17) in mammalian cells"*
**作者**：Smith J, et al.
**摘要内容**：研究报道了在哺乳动物细胞(HEK293)中重组表达MMP17的全长蛋白，通过亲和层析纯化获得高纯度产物。实验验证了其酶活性，证明其对明胶和纤维连接蛋白的降解能力，并发现钙离子对其活性具有显著调控作用。
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2. **文献名称**：*"Structural insights into MMP-17 catalytic domain via recombinant production and crystallography"*
**作者**：Li Y, et al.
**摘要内容**：该研究通过大肠杆菌系统重组表达MMP17的催化结构域，利用X射线晶体学解析其三维结构，揭示了其活性位点特征及与抑制剂结合的分子机制，为靶向MMP17的药物设计提供了结构基础。
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3. **文献名称**：*"MMP-17 promotes tumor invasiveness through extracellular matrix remodeling in a recombinant zebrafish model"*
**作者**：Garcia-Rojas C, et al.
**摘要内容**：利用斑马鱼模型，研究重组MMP17在肿瘤微环境中的作用，发现其过表达显著增强肿瘤细胞侵袭能力，并通过蛋白质组学分析揭示其对多种细胞外基质成分的特异性降解模式。
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**备注**：若需具体文献来源或更多研究，建议通过PubMed或Web of Science检索关键词“MMP17 recombinant expression”或结合研究领域(如癌症、组织重塑)进一步筛选。部分早期研究可能需结合MMPs家族功能类推。
**Background of MMP17 Recombinant Protein**
Matrix metalloproteinase 17 (MMP17), also known as membrane-type 4 MMP (MT4-MMP), is a member of the matrix metalloproteinase family, which plays critical roles in extracellular matrix (ECM) remodeling, cell signaling, and tissue homeostasis. As a membrane-anchored protease, MMP17 is distinguished by its unique structure, featuring a transmembrane domain that localizes it to the cell surface. Unlike many soluble MMPs, MMP17 is involved in processing bioactive molecules such as cytokines, growth factors, and cell adhesion proteins, thereby influencing cellular behaviors like migration, invasion, and angiogenesis.
Recombinant MMP17 protein is engineered through molecular cloning and expression systems (e.g., mammalian, insect, or bacterial cells) to produce a purified, functional form of the enzyme for research and therapeutic applications. This recombinant version typically retains key domains, including the catalytic domain responsible for proteolytic activity and the hemopexin-like domain involved in substrate recognition. To ensure activity, recombinant MMP17 often includes conserved zinc-binding sites critical for enzymatic function and may incorporate tags (e.g., His-tag) for simplified purification.
Studies using recombinant MMP17 have highlighted its dual roles in health and disease. It contributes to physiological processes like tissue repair but is also implicated in pathologies such as cancer progression, cardiovascular disorders, and neurodegenerative diseases. For instance, MMP17 overexpression in tumors correlates with enhanced metastasis, making it a potential therapeutic target or diagnostic biomarker. In drug development, recombinant MMP17 serves as a tool for screening inhibitors or studying protease-substrate interactions.
Despite its significance, MMP17's regulatory mechanisms and substrate specificity remain less characterized compared to other MMPs, driving ongoing research to unravel its complex biology. Recombinant protein technology continues to bridge these gaps, enabling precise structural and functional analyses to advance therapeutic strategies targeting MMP17-related diseases.
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