| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP26 |
| Uniprot No | Q9NRE1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 90-261aa |
| 氨基酸序列 | T SISPGRCKWN KHTLTYRIIN YPHDMKPSAV KDSIYNAVSI WSNVTPLIFQ QVQNGDADIK VSFWQWAHED GWPFDGPGGI LGHAFLPNSG NPGVVHFDKN EHWSASDTGY NLFLVATHEI GHSLGLQHSG NQSSIMYPTY WYHDPRTFQL SADDIQRIQH LYGEKCSSDI P |
| 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MMP26重组蛋白的3-4篇参考文献示例(注：文献信息为模拟概括，可能不对应真实发表论文)：
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1. **"Characterization of recombinant human MMP-26: Expression, activation, and substrate specificity"**
*作者：Park H. et al. (2003)*
**摘要**：首次报道了MMP26重组蛋白在大肠杆菌中的高效表达及纯化方法，分析了其酶活性对明胶和Ⅳ型胶原的降解能力，并探讨其在前列腺组织中的潜在病理作用。
2. **"MMP-26 promotes tumor cell proliferation and invasion in prostate cancer"**
*作者：Marchenko G.N. et al. (2004)*
**摘要**：研究通过重组MMP26蛋白实验，证明其通过降解细胞外基质成分(如纤维连接蛋白)促进肿瘤细胞侵袭，并与TIMP-4抑制剂的相互作用可能影响肿瘤进展。
3. **"Recombinant MMP-26 enzymatic activity and its regulation by TIMPs"**
*作者：Uria J.A., López-Otín C. (2005)*
**摘要**：系统分析了重组MMP26的酶动力学特性，发现其对短肽荧光底物的高效水解活性，并揭示其与其他基质金属蛋白酶抑制剂(TIMPs)的独特结合模式。
4. **"MMP-26: A novel target for cancer therapy via recombinant protein-based inhibitor screening"**
*作者：Zhao Y. et al. (2010)*
**摘要**：利用重组MMP26蛋白筛选天然化合物库，发现小分子抑制剂X可特异性阻断其酶活性，为靶向MMP26的抗癌药物开发提供了实验依据。
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以上内容综合了MMP26重组蛋白的表达、功能及应用研究的关键方向，具体文献需通过学术数据库(如PubMed)以关键词“MMP26 recombinant”检索核实。
**Background of MMP26 Recombinant Protein**
MMP26 (matrix metalloproteinase-26), also known as matrilysin-2 or endometase, is a member of the matrix metalloproteinase (MMP) family, which plays critical roles in extracellular matrix (ECM) remodeling, tissue repair, and cell signaling. Discovered in 2000. MMP26 is one of the smallest MMPs, encoded by the *MMP26* gene located on human chromosome 11. Unlike most MMPs, it lacks a hemopexin-like domain but retains the conserved catalytic domain, enabling proteolytic activity.
MMP26 is expressed in normal tissues, including the endometrium, placenta, and epithelial cells, but is also upregulated in cancers (e.g., prostate, breast, and lung), where it contributes to tumor progression, angiogenesis, and metastasis by degrading ECM components (e.g., collagen IV, fibronectin) and regulating bioactive molecules like cytokines. Its dual role in physiological processes (e.g., menstrual cycle, wound healing) and pathological conditions has driven interest in studying its molecular mechanisms.
Recombinant MMP26 protein is produced via heterologous expression systems (e.g., *E. coli*, mammalian cells) for functional studies. Purification techniques, such as affinity chromatography with His-tags, ensure high purity and activity. Researchers use the recombinant protein to investigate substrate specificity, enzymatic kinetics, and interactions with endogenous inhibitors (TIMPs) or synthetic inhibitors. It also serves as a tool for drug discovery, aiming to develop MMP26-targeted therapies for cancer and inflammatory diseases.
Despite its low basal expression, MMP26’s unique structure, substrate profile, and disease associations make it a compelling subject for biomedical research, with potential applications in diagnostics and therapeutics.
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