General Notes
Recombinant Human MMP-3Matrix metalloproteinase-3 (MMP-3), also known as stromelysin-1 (SL-1) and transin-1 is a member of the metzincins superfamily of proteases and is produced by various cells and tissues including the endothelium, vascular smooth muscle cells intima and platelets (Cui et al. 2017). MMP-3 is largely expressed by connective and vascular tissues and cells due to its roles in extracellular matrix remodeling. It is synthesized as a pre-proenzyme before being processed to remove the signal peptide forming the 57 kDa pro-MMP-3. This is then further cleaved by proteolytic enzymes to create the 45 kDa active form. Like other MMPs, MMP-3 plays a major role in tissue remodeling through the promotion of extracellular matrix (ECM) protein turnover. Specifically MMP-3 degrades the collagen proteins, type II, IV, IX as well as the proteoglycans elastin fibronectin and laminin (Cui et al. 2017). Through the degradation of these ECM components, growth factors and adhesion molecules, MMP-3 can modify the extracellular environment and modulate cell to cell signaling. As such, MMP-3 is implicated in synaptic plasticity through enzymatic modification of ECM constituents (Lech et al. 2019).This recombinant Human MMP-3 can be used to create a standard curve in a sandwich ELISA with purified Mouse anti Human MMP-3 antibody, clone I08-9G7 (MCA6258GA) as a capture antibody and biotinylated Mouse anti Human MMP-3 antibody, clone G05-6A10 (MCA6259B) as the detection antibody.
