Mouse Monoclonal Antibody
MA1-772 contains 100 μg of in vitro produced, protein A purified antibody (1 mg/mL) in PBS containing 1 mg/mL BSA and 0.05% sodium azide. MA1-772 detects MMP-2 from human and rat samples. MA1-772 has been successfully used in Western blot applications. By Western blot, MA1-772 detects a ~50 kDa band representing MMP-2 from WI-38 cell lysate or rat lung samples. The MA1-772 immunogen is a synthetic peptide corresponding to residues T(557) S L G L P P D V Q R V D(569) of human MMP-2. MA1-772 has been successfully used in western blotting and ELISA analysis of MMP2 in human and rat samples. By Western blot, MA1-772 detects a ~74 kDa band representing MMP2 in MCF7 and HT-1080 cell lysate or rat lung.
MMP (matrix metalloproteinase) are proteolytic enzymes capable of degrading connective tissue components. MMP have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). MMPa and TIMPs play a significant role in regulating angiogenesis. MMP2 is synthesized as a 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids, and contains the basic structure of propeptide, catalytic, and hemopexin domains. The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. Functionally, MMP2 is involved in tissue remodeling. Mutations in MMP-2 gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms of MMP-2 have been found. Trusted Sustainability Partner
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