MMP2 Mouse anti-Human, Clone: OTI4B11, lyophilized, TrueMAB™

Description

• Reconstitute with PBS (pH 7.3) and recommend to perform another round of desalting process using Product No
• 7KMWCO 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.