In Abcam's MMP-3 Activity Assay Kit, MMP-3 hydrolyzes a specific FRET substrate to release the quenched fluorescent group Mca, which can be detected fluorometrically at Ex/Em=325/393 nm.
Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 (PubMed:11029580, PubMed:1371271). Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway (PubMed:2383557). Acts also intracellularly (PubMed:22265821). For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed:21330369). In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1 (PubMed:35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed:35940311).
STMY1, MMP3, Stromelysin-1, SL-1, Matrix metalloproteinase-3, Transin-1, MMP-3
In Abcam's MMP-3 Activity Assay Kit, MMP-3 hydrolyzes a specific FRET substrate to release the quenched fluorescent group Mca, which can be detected fluorometrically at Ex/Em=325/393 nm.
In Abcam's MMP-3 Activity Assay Kit, MMP-3 hydrolyzes a specific FRET substrate to release the quenched fluorescent group Mca, which can be detected fluorometrically at Ex/Em=325/393 nm. The kit provides a rapid, simple, sensitive and reliable test which can also be used as a high throughput assay of MMP-3 activity. The assay sensitivity is < 50 μU.
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This product is manufactured by BioVision, an Abcam company and was previously called K783 MMP-3 Activity Fluorometric Assay Kit. K783-100 is the same size as the 100 test size of ab118972.
The matrix metalloproteinase-3 (MMP-3, stromelysin-1) exhibits a number of activities that would make it a particularly good tumor promoter. Like several other MMPs, MMP-3 was first cloned and later recloned as a cancer-specific gene. In addition to degrading numerous extracellular matrix components, MMP-3 can activate gelatinase B, the collagenases and several serpin-type serine proteinase inhibitors. Moreover, it can release a number of cell surface molecules, including E-cadherin, a known contributor to cancer development.
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MMP3 also known as stromelysin-1 is a member of the matrix metalloproteinase (MMP) family. These proteins are zinc-dependent endopeptidases. MMP3 specifically has a molecular weight of approximately 54 kDa and is responsible for degrading extracellular matrix components such as collagen fibronectin and laminin. MMP3 is expressed in various tissues including fibroblasts chondrocytes and endothelial cells. It plays a significant role in tissue remodeling wound healing and potentially aids in the breakdown of cellular matrices.
MMP3 contributes to multiple physiological and pathological processes. It supports the remodeling of connective tissues and assists in normal developmental processes. MMP3 can work as part of a complex with other MMP proteins which can enhance or inhibit its activity. The balance of MMPs including MMP3 regulates the extracellular matrix turnover and is important for maintaining tissue homeostasis.
MMP3 participates in pathways involved in tissue remodeling and inflammatory responses. It is part of cellular pathways regulated by cytokines like interleukin-1 (IL-1) and tumor necrosis factor-alpha (TNF-alpha). These pathways link MMP3 to other proteins such as MMP1 and MMP9 which perform overlapping and distinct roles in matrix degradation during inflammation and tissue repair.
MMP3 is implicated in conditions like arthritis and cardiovascular diseases. MMP3 contributes to cartilage degradation in rheumatoid arthritis and is associated with the breakdown of vascular structures in atherosclerosis. Proteins like MMP9 and MMP13 often interact with MMP3 in these pathological conditions forming a network that exacerbates tissue damage and disease progression.
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MMP-3 Positive Control
MMP-3 Mca Standard
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