MMP-12 was first described in murine macrophages, later in human macrophages, and more recently in other cell types. Also known as metalloelastase, MMP-12 is able to degrade elastin, entactin, laminin-1, fibronectin, type IV collagen as well as insulin B-chain and casein. MMP-12 is often confused with the Serine proteinase, Leukocyte elastase (EC 3.4.21.37) because of similar nomenclature. MMP-12 is structurally similar to the classical MMPs (MMP-1, MMP-3); it contains a propeptide with autoinhibitory cysteine switch site, a well conserved zinc site, hinge region and hemopexin domain. MMP-12 lacks a transmembrane domain and furin cleavage site. The zymogen for MMP-12 is about 54 Kd, and is quickly activated to the 45 Kd form, and this breaks down to cascade of active forms, ending with the common 22 Kd form. RP1MMP12 Anti-MMP-12 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 54 Kd, 45 Kd, and 22 Kd. RP1MMP12 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Stimulated macrophages produce MMP-12; it has also been found in osteosarcoma cells, synovial fibroblasts and lung fibroblasts. MMP-12 levels in quiescent cells and tissues are minimal (with the exception of macrophages), and mitogen stimulation or protein concentration is often needed to visualize the bands. In addition, cell types differ greatly in the quantity of MMP-12 produced. 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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