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MMP2 Mouse anti-Human, Clone: MMP2/2C1-1D12, Invitrogen™

Mouse Monoclonal Antibody

Manufacturer:  Invitrogen MA1779

Catalog No. 01-674-564

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MA1-779 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. MA1-779 has been successfully used in Western blot applications. By Western blot, MA1-779 detects a ~66 kDa band representing purified recombit human MMP-2. The MA1-779 immunogen is activated rhMMP-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.


1 mg/mL
PBS with 1mg/mL BSA and 0.05% sodium azide
Matrix metalloproteinase-2
IgG1, kappa
100 μg
-20° C, Avoid Freeze/Thaw Cycles
ELISA, Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blot
Activated rhMMP-2
Protein A
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