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PA1-25205 detects MMP-2, free or bound to TIMP2, from human samples. This antibody does not cross-react with other MMP family members. PA1-25205 recognizes only the latent form of MMP2, and therefore may be used to distinguish the zymogen from the active enzyme.
PA1-25205 has been successfully used in immunoprecipitation, immunohistochemistry (frozen), ELISA, and Western blot procedures.
The PA1-25205 immunogen is a synthetic peptide corresponding to the propeptide domain of human MMP-2.
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.
仅用于科研。不用于诊断过程。未经明确授权不得转售。