Matrix metalloproteinases (MMPs) are highly homologous Zn2+ endopeptidases involved in extracellular matrix (ECM) breakdown. MMP-20 (enamelysin) is involved in the degradation of various components of the ECM during development, hemostasis and pathological conditions. The domain organization of MMP-20 is similar to other MMPs, including a signal peptide, a prodomain with the conserved motif PRCGVPD involved in maintaining enzyme latency, a catalytic domain with a Zn-binding site, and a COOH-terminal fragment similar to the sequence of hemopexin. MMP-20 is expressed during the early through middle stages of enamel development at which time it likely hydrolyzes Amelogenin, a major protein component of the enamel matrix. The expression pattern of MMP-20 in the enamel organ indicates that it may be involved in the turnover of ECM proteins during tooth development and enamel formation. Human MMP-20 maps to chromosome 11q22.3, clustered to at least seven other members of the MMP gene family.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
MMP20 polyclonal antibody detects endogenous levels of MMP20 protein.
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