MMP7
GeneName
MMP7
Summary
MMP7, also known as MMP-7 or matrix metalloproteinase-7, is a 30kDa enzyme that is secreted into the extracellular matrix and space. It plays a critical role in the degradation of various components of the extracellular matrix, particularly collagen, and is involved in processes such as extracellular matrix organisation and disassembly. MMP7 exhibits endopeptidase activity and is capable of binding zinc ions, which is essential for its enzymatic function. It is also implicated in defence responses against Gram-negative and Gram-positive bacteria, and its activity can positively regulate cell migration, making it important in tissue remodelling and repair.
Importance
MMP7 is relevant to: - Cancer progression and metastasis due to its role in extracellular matrix remodelling and tumour microenvironment modification - Wound healing processes as it facilitates tissue repair and regeneration - Inflammatory diseases where it contributes to tissue damage and remodelling - Host defence mechanisms against bacterial infections through its antibacterial peptide secretion and activity
Top Products
For researchers investigating MMP7, we highly recommend the top-selling recombinant antibody, Anti-MMP7 antibody [EPR17888-101] (ab205525). This antibody has been validated in knockout models, ensuring its reliability for your experiments. It is suitable for a variety of applications, most notably Western blotting (WB) and immunohistochemistry (IHC), making it a versatile choice for detecting MMP7 in different sample types. With 29 citations, this antibody is well-regarded in the research community, reflecting its effectiveness and trustworthiness in MMP7 studies.
Abcam Product Citation Summary
The data indicates a strong focus on the role of MMP7 in human prostate cancer, with multiple studies employing various applications such as Western blotting, immunohistochemistry, and immunofluorescence. The studies explore the effects of p14ARF overexpression and knockdown, as well as cell migration. Additionally, MMP7 is investigated in the context of human HCC cells and breast cancer cell lines, highlighting its potential involvement in cancer-related signalling pathways.
Abcam Product Citation Table
Domain
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Function
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.
Sequence Similarities
Belongs to the peptidase M10A family.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
Alternative names
MPSL1, PUMP1, MMP7, Matrilysin, Matrin, Matrix metalloproteinase-7, Pump-1 protease, Uterine metalloproteinase, MMP-7