| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP13 |
| Uniprot No | P45452 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 104-274aa |
| 氨基酸序列 | YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM LPDDDVQGIQSLYGPGDEDPN |
| 预测分子量 | 21 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MMP13重组蛋白的参考文献示例(虚构内容，仅作格式参考)：
1. **文献名称**：*Expression and Purification of Recombinant MMP13 in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究描述了一种高效在大肠杆菌中表达并纯化重组MMP13蛋白的方法，通过优化诱导条件及亲和层析技术获得高活性蛋白酶，适用于体外酶动力学研究。
2. **文献名称**：*Structural Insights into MMP13 Substrate Specificity by Crystallography*
**作者**：Brown C, et al.
**摘要**：通过X射线晶体学解析了重组MMP13的活性位点结构，揭示了其与胶原底物结合的关键氨基酸残基，为设计特异性抑制剂提供依据。
3. **文献名称**：*MMP13 Recombinant Protein in Osteoarthritis Model*
**作者**：Lee H, et al.
**摘要**：利用重组MMP13蛋白在骨关节炎小鼠模型中验证其降解Ⅱ型胶原的能力，证明其参与软骨退变的病理机制。
4. **文献名称**：*Development of a High-Throughput Assay for MMP13 Activity*
**作者**：Wang Y, et al.
**摘要**：基于荧光标记底物和重组MMP13蛋白，开发了一种高通量活性检测方法，用于筛选潜在的治疗性抑制剂。
(注：以上文献信息为示例，实际引用请通过PubMed或学术数据库检索真实文献。)
Matrix metalloproteinase 13 (MMP13), also known as collagenase-3. is a member of the zinc-dependent endopeptidase family involved in extracellular matrix (ECM) remodeling. It specifically cleaves type II collagen, a major structural component of cartilage, making it a critical enzyme in physiological processes like tissue repair, embryonic development, and bone growth. However, dysregulation of MMP13 is implicated in pathological conditions, including osteoarthritis, rheumatoid arthritis, cancer metastasis, and chronic wounds, where excessive collagen degradation disrupts tissue integrity.
Recombinant MMP13 protein is produced using genetic engineering techniques, typically by expressing the human MMP13 gene in prokaryotic (e.g., E. coli) or eukaryotic (e.g., mammalian or insect) systems. The protein is often generated as a pro-enzyme (zymogen) requiring activation, such as through cleavage by proteases like trypsin or organomercurials. Post-translational modifications, critical for its catalytic activity, are better preserved in eukaryotic expression systems. The recombinant protein includes domains essential for function: a pro-peptide, catalytic domain with a conserved zinc-binding motif, and a hemopexin-like domain for substrate recognition.
Research applications of recombinant MMP13 include studying its enzymatic mechanisms, substrate specificity, and interactions with inhibitors. It serves as a tool for drug discovery, particularly in developing selective inhibitors for arthritis therapy. For instance, small-molecule inhibitors (e.g., CL-82198) and monoclonal antibodies targeting MMP13 have entered clinical trials. Additionally, it aids in modeling ECM remodeling in 3D cell cultures or disease models. Despite challenges in avoiding off-target effects due to structural similarities among MMPs, MMP13 remains a prioritized therapeutic target owing to its central role in cartilage degradation pathologies.
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