Use

MMP-20, first described in bovine dental pulp, is a classical type-I collagenase; like MMP-1 it is able to cleave intact type-I collagen at the same site in all three strands. The sequence for MMP-8 is similar to MMP-1, but until recently it was thought to be produced exclusively by dental pulp. MMP-20 has recently been detected in other cell types. The zymogen for MMP-20 is about 58 Kd, and is quickly activated to the 45 Kd form, and this breaks down to a cascade of active forms. RP4MMP20 recognizes the Propeptide region, which is removed during enzymatic activation. The antibody can be used to discriminate between the zymogen and activated MMP-20. RP4MMP20 anti-MMP-20 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 58 Kd. RP4MMP20 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Most cell types do not produce MMP-20; it has been found in osteosarcoma cells, HeLa cells, and gingival fibroblasts. MMP-20 levels in quiescent cells and tissues are minimal (with the exception of dental pulp), and mitogen stimulation or protein concentration is often needed to visualize the bands. In addition, cell types differ greatly in the quantity of MMP-20 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.

FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS.

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