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MMP2 Mouse anti-Human, Mouse, Porcine, Rat, Clone: 2B10D1, Proteintech

Mouse Monoclonal Antibody
Supplier: Proteintech Group Inc 663661IG150UL

Description
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.Specifications
MMP2 | |
Monoclonal | |
1 mg/mL | |
PBS with 50% glycerol and 0.02% sodium azide; pH 7.3 | |
P08253, P33434, P33436 | |
Mmp2 | |
MMP2 Fusion Protein Ag25039 | |
150 μL | |
Primary | |
Human, Mouse, Pig, Rat | |
Antibody | |
IgG1 |
Immunohistochemistry (Paraffin), Western Blot | |
2B10D1 | |
Unconjugated | |
MMP2 | |
72 kDa gelatinase, 72 kDa type IV collagenase, CLG4, CLG4A, Gelatinase A, Matrix metalloproteinase 2, MMP 2, MMP II, MMP2, MONA, TBE 1 | |
Mouse | |
Protein G | |
RUO | |
17390, 397391, 4313, 81686 | |
-20°C | |
Liquid |
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