Alternative names of antibody target:
MMP9, MMP-9, MMP 9, Matrix metalloproteinase-9, Matrix metalloproteinase 9, Gelatinase B, 92kDa type IV collagenase
The mammalian Matrix metalloproteinases (MMPs) degrade extracellular matrix in physiological and pathological processes. After cleavage of a single peptide domain of about 20 amino acids, the MMPs are secreted in latent forms. Upon activation, the N-terminal propeptide domain is cleaved to generate the active forms of MMP. MMP-9 (92 kDa type IV collagenase, Gelatinase-B) contains the basic structure of propeptide, catalytic, and hemopexin domains. It is an important proteinase in tissue remodeling.
This antibody reacts with:
E. coli-expressed active rat 92-kDa type IV collagenase
Concentration of antibody:
Formulation of this antibody:
100 µg (0.5 mg/ml) affinity purified rabbit anti-rat MMP-9 polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 50% glycerol, 1% BSA, 0.02% thimerosal.
This antibody has been succesfully tested for use in following methods:
Western blot, Immunoprecipitation, Immunohistochemistry
Western blot analysis (0.5-4 µg/ml), immunoprecipitation (4-8 µg/ml), and Immunohistochemistry (20-40 µg/ml). However, the optimal conditions should be determined individually.