纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MMP1 |
Uniprot No | P03956 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 20-469aa |
氨基酸序列 | FPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQE FFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIE NYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHR DNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHE LGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQP IGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISV FWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFG FPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDF PGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN HHHHHHHHHH |
预测分子量 | 53 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MMP1重组蛋白的3篇文献示例(内容为模拟示例,非真实文献):
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1. **文献名称**: *Expression and purification of recombinant human MMP1 in Escherichia coli for structural studies*
**作者**: Smith J, et al.
**摘要**: 该研究报道了利用大肠杆菌表达系统高效表达重组人源MMP1的优化方法,并通过亲和层析纯化获得高纯度蛋白,用于X射线晶体学分析其三维结构。
2. **文献名称**: *Functional characterization of recombinant MMP1 in tumor invasion models*
**作者**: Lee H, et al.
**摘要**: 研究通过昆虫细胞表达系统制备重组MMP1.并验证其在体外降解Ⅰ型胶原的能力,进一步证明其在肿瘤细胞侵袭实验中对基底膜的破坏作用。
3. **文献名称**: *Role of recombinant MMP1 in wound healing: In vivo and in vitro evidence*
**作者**: Garcia R, et al.
**摘要**: 利用哺乳动物细胞表达的重组MMP1.研究发现其可通过调控细胞外基质重塑促进皮肤创伤修复,并揭示了其在成纤维细胞迁移中的关键作用。
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(注:以上文献信息为示例,实际引用请通过PubMed、Web of Science等数据库检索真实文献。)
Matrix metalloproteinase-1 (MMP1), also known as interstitial collagenase, is a member of the zinc-dependent endopeptidase family involved in extracellular matrix (ECM) remodeling. Discovered in the 1960s, MMP1 specifically cleaves fibrillar collagens (types I, II, III), key structural components of connective tissues, initiating their degradation during physiological and pathological processes. Its activity is tightly regulated at transcriptional, post-translational, and inhibitory levels (e.g., TIMPs) to prevent excessive tissue damage.
Structurally, MMP1 consists of a signal peptide, pro-domain, catalytic domain, and hemopexin-like C-terminal domain. The pro-domain maintains latency until proteolytic activation, while the catalytic domain houses the conserved Zn²⁺-binding motif essential for enzymatic function. Recombinant MMP1 is typically produced in Escherichia coli or mammalian expression systems, engineered with tags (e.g., His-tag) for purification. This engineered protein retains collagenolytic activity when refolded or secreted in soluble form, enabling controlled experimental use.
In research, recombinant MMP1 serves as a critical tool to study tissue remodeling in wound healing, embryonic development, and diseases like cancer metastasis, osteoarthritis, and pulmonary fibrosis. It facilitates drug discovery by screening MMP inhibitors and modeling pathological ECM degradation in vitro. Dysregulated MMP1 expression correlates with tumor invasiveness and poor prognosis, highlighting its dual role as a repair mediator and disease driver. Current challenges include understanding context-dependent regulatory mechanisms and developing isoform-specific therapeutics to minimize off-target effects.
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