| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMP11 |
| Uniprot No | P24347 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 98-488aa |
| 氨基酸序列 | FVL SGGRWEKTDL TYRILRFPWQ LVQEQVRQTM AEALKVWSDV TPLTFTEVHE GRADIMIDFA RYWHGDDLPF DGPGGILAHA FFPKTHREGD VHFDYDETWT IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR YPLSLSPDDC RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA QGHIWFFQGA QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI YFFRGRDYWR FHPSTRRVDS PVPRRATDWR GVPSEIDAAF QDADGYAYFL RGRLYWKFDP VKVKALEGFP RLVGPDFFGC AEPANTFL |
| 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MMP11重组蛋白的3篇代表性文献概览(文献标题、作者及摘要内容简述)：
---
1. **标题**: *"Expression and characterization of recombinant human matrix metalloproteinase 11 (MMP-11) in mammalian cells"*
**作者**: Pei D, Weiss SJ
**摘要**: 本研究利用哺乳动物细胞表达系统(如CHO细胞)成功表达并纯化了具有酶活性的重组人MMP11蛋白。通过体外实验验证其底物特异性，发现其能够降解细胞外基质成分(如IV型胶原和层粘连蛋白)，并讨论了其在肿瘤微环境中的潜在作用。
---
2. **标题**: *"Purification and functional analysis of recombinant MMP-11: Role in adipocyte differentiation"*
**作者**: Maquoi E, et al.
**摘要**: 研究通过大肠杆菌表达系统获得重组MMP11蛋白，优化了纯化流程以提高蛋白稳定性。功能实验表明，重组MMP11通过调节脂肪细胞分化相关信号通路(如TGF-β)，影响前脂肪细胞的分化过程，提示其在代谢疾病中的调控作用。
---
3. **标题**: *"Development of a high-yield MMP-11 production system in Pichia pastoris and its application in cancer invasion assays"*
**作者**: Li Y, et al.
**摘要**: 采用毕赤酵母表达系统高效分泌表达重组MMP11.优化发酵条件后获得高纯度蛋白。利用该蛋白进行体外肿瘤细胞侵袭实验，证实MMP11通过降解细胞外基质促进肿瘤细胞迁移，为靶向MMP11的抗癌药物开发提供实验模型。
---
**备注**：以上文献为示例性内容，实际引用时需根据具体研究需求检索PubMed、Web of Science等数据库获取真实文献。
Matrix metalloproteinase 11 (MMP11), also known as stromelysin-3. is a member of the MMP family of zinc-dependent endopeptidases involved in extracellular matrix (ECM) remodeling. Discovered in 1990. MMP11 is distinct from other MMPs due to its unique expression pattern and substrate preferences. Unlike many MMPs secreted by epithelial or tumor cells, MMP11 is primarily produced by stromal fibroblasts in response to inflammatory cytokines, growth factors, or tumor-stroma interactions. Structurally, it consists of a pro-domain, catalytic domain, and a hemopexin-like domain, though it lacks the transmembrane domain found in membrane-type MMPs.
Functionally, MMP11 plays dual roles in physiological and pathological processes. In normal conditions, it contributes to tissue homeostasis, wound healing, and embryonic development by processing ECM components and bioactive molecules. However, its dysregulation is strongly implicated in cancer progression. MMP11 does not directly degrade major ECM structural proteins (e.g., collagens) but processes ECM-associated signaling molecules, adhesion proteins, and protease inhibitors to create a tumor-permissive microenvironment. It facilitates tumor cell invasion, immune evasion, and angiogenesis while suppressing apoptosis. Elevated MMP11 expression correlates with poor prognosis in breast, colorectal, and gastric cancers.
Recombinant MMP11 protein is engineered using mammalian expression systems (e.g., CHO cells) to ensure proper post-translational modifications and enzymatic activity. This tool enables researchers to study MMP11's substrate specificity, regulatory mechanisms, and interactions with inhibitors. It serves as a critical reagent for developing diagnostic biomarkers and therapeutic agents targeting MMP11-driven pathologies. Current research explores its potential as a predictive biomarker for chemotherapy response and a target for stromal reprogramming strategies in cancer treatment. However, challenges remain in understanding its context-dependent roles and designing selective inhibitors to minimize off-target effects on other MMPs.
×
