| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP7 |
| Uniprot No | P09237 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-267aa |
| 氨基酸序列 | LPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFG LPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYT RDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSY PFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELG HSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNS |
| 预测分子量 | 28 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MMP7重组蛋白的3篇代表性文献的简要总结(根据领域知识构造，非真实文献)：
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1. **文献名称**：Recombinant expression and functional characterization of human matrix metalloproteinase-7 in Escherichia coli
**作者**：Smith A, et al.
**摘要**：该研究报道了通过大肠杆菌表达系统高效表达人源MMP7重组蛋白的优化方法，并通过亲和层析纯化获得高活性蛋白。实验验证了重组MMP7对胶原和明胶底物的水解活性，为后续体外功能研究提供了工具。
2. **文献名称**：MMP7 promotes tumor invasion through cleavage of extracellular matrix proteins in colorectal cancer
**作者**：Zhang L, et al.
**摘要**：通过体外实验验证重组MMP7蛋白能够降解细胞外基质成分(如纤维连接蛋白和层粘连蛋白)，并证明其过表达促进结直肠癌细胞侵袭。研究揭示了MMP7在肿瘤转移中的关键作用机制。
3. **文献名称**：Development of a fluorescence-based assay for screening MMP7 inhibitors using recombinant enzyme
**作者**：Kim H, et al.
**摘要**：本研究利用重组MMP7蛋白建立了一种高通量荧光底物检测方法，用于筛选潜在抑制剂。通过结构活性关系分析，发现两种小分子化合物可显著抑制MMP7的酶活性，为靶向治疗提供了候选分子。
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*注：以上文献为示例性内容，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。*
**Background of MMP7 Recombinant Protein**
Matrix metalloproteinase 7 (MMP7), also known as matrilysin, is a member of the MMP family of zinc-dependent endopeptidases involved in extracellular matrix (ECM) remodeling. Unlike other MMPs, MMP7 lacks a hemopexin-like domain, making it one of the smallest and most compact enzymes in the family. It is primarily secreted by epithelial cells, fibroblasts, and immune cells, and plays critical roles in tissue repair, inflammation, and cancer progression.
MMP7 is synthesized as an inactive zymogen (pro-MMP7) that requires proteolytic cleavage for activation. Its substrate specificity includes ECM components like fibronectin, elastin, and proteoglycans, as well as non-matrix proteins such as pro-tumor necrosis factor-alpha (pro-TNF-α) and E-cadherin. This broad activity links MMP7 to processes like wound healing, cell migration, and immune regulation.
Recombinant MMP7 is produced using expression systems (e.g., *E. coli* or mammalian cells*) to generate high-purity, bioactive protein for research and therapeutic applications. Its production typically involves cloning the MMP7 gene into expression vectors, followed by purification via affinity chromatography.
In disease contexts, MMP7 is upregulated in cancers (e.g., colorectal, breast) where it promotes tumor invasion, metastasis, and angiogenesis. It also contributes to inflammatory conditions (e.g., rheumatoid arthritis, fibrosis) by modulating cytokine activity and tissue remodeling. Conversely, MMP7's role in ECM turnover has sparked interest in regenerative medicine and drug development, with inhibitors explored as potential therapeutics.
As a biomarker, MMP7 levels in serum or tissues are studied for diagnostic or prognostic value in cancer and fibrotic diseases. Its dual role as a pathogenic driver and repair mediator underscores the complexity of targeting MMP7 in clinical settings.
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