MMP20 polyclonal antibody

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) .

Western blot (WB) analysis of MMP20 polyclonal antibody at 1:500 dilution Lane1:HEK293T whole cell lysate Lane2:Raw264.7 whole cell lysate Lane3:PC12 whole cell lysate