| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP9 |
| Uniprot No | P14780 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 107-707aa |
| 氨基酸序列 | FQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED |
| 预测分子量 | 68.6kDa |
| 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MMP9重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Biochemical characterization of recombinant human matrix metalloproteinase 9 (MMP9) expressed in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：该研究报道了在大肠杆菌中高效表达并纯化重组人MMP9的方法，通过体外酶活性实验证实其具有明胶降解能力，并分析了金属离子依赖性对酶活性的影响。
2. **文献名称**：*Glycosylation of human matrix metalloproteinase-9 (MMP9) modulates its function*
**作者**：Van den Steen PE, et al.
**摘要**：作者利用哺乳动物系统表达重组MMP9.发现糖基化修饰显著影响其酶活性和稳定性，并揭示了不同糖型在炎症微环境中的功能差异。
3. **文献名称**：*Recombinant MMP9 promotes tumor cell invasion by cleaving extracellular matrix proteins in a 3D model*
**作者**：Deryugina EI, et al.
**摘要**：研究利用重组MMP9处理三维胶原模型，证明其通过降解IV型胶原和层粘连蛋白增强肿瘤细胞侵袭能力，提示MMP9在癌症转移中的关键作用。
4. **文献名称**：*Structural insights into the propeptide-mediated regulation of MMP9 activity*
**作者**：Mantuano E, et al.
**摘要**：通过X射线晶体学解析重组MMP9与其前肽的复合物结构，阐明了前肽在酶原激活和底物识别中的调控机制，为靶向抑制剂设计提供依据。
这些文献涵盖了重组MMP9的表达纯化、翻译后修饰、病理功能及结构机制，适用于基础研究与药物开发参考。
Matrix metalloproteinase 9 (MMP9), also known as 92 kDa type IV collagenase or gelatinase B, is a zinc-dependent endopeptidase belonging to the matrix metalloproteinase (MMP) family. It plays a critical role in extracellular matrix (ECM) remodeling by degrading structural proteins such as collagen IV, gelatin, and elastin. MMP9 is synthesized as an inactive zymogen (pro-MMP9) containing a propeptide domain that must be cleaved for activation. Its multidomain structure includes a catalytic domain with a zinc-binding site, fibronectin-like repeats for substrate binding, and a hemopexin-like domain influencing cellular interactions and substrate specificity.
Physiologically, MMP9 participates in tissue repair, angiogenesis, and immune responses, but its dysregulation is linked to pathological conditions including cancer metastasis, chronic inflammation, cardiovascular diseases, and neurodegenerative disorders. In cancer, MMP9 facilitates tumor invasion by breaking down basement membranes and releasing growth factors from the ECM. It is highly expressed in neutrophils, macrophages, and tumor-associated stromal cells under inflammatory or hypoxic conditions.
Recombinant MMP9 protein is produced using expression systems like mammalian cells (e.g., HEK293. CHO) or insect cells to ensure proper post-translational modifications. Purification typically involves affinity chromatography (e.g., His-tag or GST-tag systems) followed by endotoxin removal for in vivo applications. Quality assessments include SDS-PAGE, Western blotting, and functional activity assays using gelatin or collagen substrates.
As a research tool, recombinant MMP9 enables studies on cell migration, ECM dynamics, and therapeutic inhibitor screening. It also serves as a potential biomarker and therapeutic target, though clinical translation faces challenges due to MMP9's structural similarity to other MMPs and pleiotropic biological roles. Current research focuses on developing selective inhibitors and understanding its context-dependent regulatory mechanisms in disease progression.
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