General Notes
Mouse anti Human MMP-2 antibody, clone J08-3B10, recognizes matrix metalloproteinase-2 also known as 72 kDa type IV collagenase, 72 kDa gelatinase and gelatinase A. MMP-2 is a member of the metzincins superfamily of proteases and is produced by various cells and tissues including the endothelium, vascular smooth muscle cells, adventitia platelets and leukocytes (Cui et al. 2017). MMP-2 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 72 kDa pro-MMP-2. Pro-MMP-2 is then recruited to the cell surface where it undergoes autocatalytic cleavage to form the active 63 kDa form. Like other MMP’s, MMP-2 plays a major role in tissue remodeling through the promotion of extracellular matrix (ECM) protein turnover. Specifically MMP-2 degrades the collagen proteins, type I, II, III, IV, V, VII, X, XI and gelatin. It is also able to target other ECM substrates including aggrecan, elastin, fibronectin and laminin (Cui et al. 2017). However a number of non-matrix proteins have been identified as targets of MMP-2, to regulate various physiological and pathophysiological processes including embryonic growth/development, angiogenesis, vascular diseases, inflammation, infective diseases and tumor progression. MMP-2 may also play a role in airway remodeling and may be responsible for the progressive decline of lung function in bronchial asthma (Kuwabara et al. 2018).The biotinylated Mouse anti Human MMP-2 antibody, clone J08-3B10 (MCA6257B) can be used as a detection antibody in a sandwich ELISA with the purified Mouse anti Human MMP-2 antibody, clone C12-8A3 (MCA6256GA) as the capture antibody.
