| 纯度 | >98%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP3 |
| Uniprot No | P08254 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 101-477aa |
| 氨基酸序列 | MRTFPGIPKW RKTHLTYRIV NYTPDLPKDA VDSAVEKALK VWEEVTPLTF SRLYEGEADI MISFAVREHG DFYPFDGPGN VLAHAYAPGP GINGDAHFDD DEQWTKDTTG TNLFLVAAHE IGHSLGLFHS ANTEALMYPL YHSLTDLTRF RLSQDDINGI QSLYGPPPDS PETPLVPTEP VPPEPGTPAN CDPALSFDAV STLRGEILIF KDRHFWRKSL RKLEPELHLI SSFWPSLPSG VDAAYEVTSK DLVFIFKGNQ FWAIRGNEVR AGYPRGIHTL GFPPTVRKID AAISDKEKNK TYFFVEDKYW RFDEKRNSME PGFPKQIAED FPGIDSKIDA VFEEFGFFYF FTGSSQLEFD PNAKKVTHTL KSNSWLNC |
| 预测分子量 | 43 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MMP3重组蛋白的3篇文献及其摘要概括：
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1. **文献名称**：*"Expression and characterization of recombinant human matrix metalloproteinase-3 (MMP-3) in Escherichia coli"*
**作者**：Li, J., Brick, P., & Murphy, G.
**摘要**：该研究报道了在大肠杆菌中高效表达重组人MMP3的方法，并通过亲和层析纯化获得高纯度蛋白。作者验证了重组MMP3的酶活性，证明其在体外可降解明胶和胶原，为后续功能研究提供可靠工具。
2. **文献名称**：*"Role of recombinant MMP3 in cartilage degradation: Insights into osteoarthritis pathogenesis"*
**作者**：Nagase, H., & Kashiwagi, M.
**摘要**：研究利用重组MMP3蛋白模拟骨关节炎微环境，发现其能显著降解软骨中的蛋白多糖和Ⅱ型胶原，提示MMP3在关节破坏中的关键作用，为靶向治疗提供理论依据。
3. **文献名称**：*"Development of a fluorescence-based assay for screening MMP3 inhibitors using recombinant protein"*
**作者**：Smith, R. D., & Schwarzbauer, J. E.
**摘要**：作者构建了基于荧光标记底物的MMP3活性检测体系，利用重组MMP3蛋白筛选小分子抑制剂，发现多个潜在化合物可特异性抑制其酶活性，为抗转移药物开发奠定基础。
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以上文献涵盖MMP3重组蛋白的表达纯化、功能机制研究及药物筛选应用方向，均为该领域的代表性研究。如需具体年份或期刊信息，可进一步补充检索。
Matrix metalloproteinase-3 (MMP3), also known as stromelysin-1. is a member of the MMP family of zinc-dependent endopeptidases involved in extracellular matrix (ECM) remodeling. It plays a critical role in physiological processes such as tissue repair, embryonic development, and angiogenesis, as well as pathological conditions including cancer metastasis, arthritis, and cardiovascular diseases. Unlike collagenases (e.g., MMP1) that primarily degrade fibrillar collagens, MMP3 exhibits broad substrate specificity, targeting proteoglycans, laminin, fibronectin, and other non-collagen ECM components. Notably, MMP3 can activate pro-forms of other MMPs (e.g., MMP9), amplifying proteolytic cascades.
Recombinant MMP3 protein is produced using expression systems like *E. coli* or mammalian cells (e.g., CHO), followed by purification via affinity chromatography. Its structure includes a pro-domain (maintaining latency), a catalytic domain with a conserved zinc-binding motif, and a hemopexin-like C-terminal domain influencing substrate recognition. For research applications, recombinant MMP3 is often supplied in an active form or as a latent pro-enzyme activated by cleavage (e.g., using APMA).
Studies leveraging recombinant MMP3 focus on elucidating ECM degradation mechanisms, screening MMP inhibitors for therapeutic development, and modeling disease progression. Dysregulated MMP3 expression correlates with tumor invasiveness, cartilage destruction in osteoarthritis, and plaque instability in atherosclerosis. However, its dual role in tissue homeostasis vs. pathology necessitates context-specific research. Recombinant proteins enable controlled in vitro studies, bypassing complexities of endogenous MMP3 regulation by TIMPs (tissue inhibitors of metalloproteinases). Current challenges include optimizing activity assays and addressing off-target effects in drug discovery.
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