MMP-19, first described, as an MMP elevated in Rheumatoid Arthritis, was later found to be produced by a wide variety of cell types under different conditions. The sequence for MMP-19 contains the canonical MMP elements of cysteine switch (PRCGL) and HExGH catalytic zinc site, without a furin cleavage site or transmembrane domain. Unlike the other MMPs. MMP-19 has an 8-residue acidic patch at the beginning of the hinge region. MMP-19 has been detected in a number of cell types, including dermal fibroblasts, lung fibroblasts and many tumor cell lines, and is expressed during development in most organs. The zymogen form of MMP-19 is found at about 58 kd. The enzyme is rapidly activated to a 55 kd form, a 45-47 kd size, then to a 28 kd final active form. Depending on the activation method, the MMP-19 can be seen as a cascade of active forms. RP2MMP19 Anti-MMP-19 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 58 Kd, 45 Kd, and a series of further cleaved active forms. RP2MMP19 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. The hemopexin domain is cleaved from the smallest active form of MMP-19, and the antibody does not see this form. MMP-19 is not constituitively produced by most cell types; it has been found in lung fibroblasts, and gingival fibroblasts when stimulated with TPA, as well as breast tumor and osteosarcoma cell lines. Cell types differ greatly in the quantity of MMP-19 produced; the conditioned media may need to be concentrated for Western blot. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for non-human samples.

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