Use

MMP-18 was first described in Xenopus during development, and is distinct from MMP-1, which it most closely resembles. MMP-18 has been shown to digest intact type-I collagen at the same site as the classical collagenases (MMP-1, MMP-8, MMP-13). RP3MMP18 Anti-MMP18 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 53 Kd and 51 Kd (the pro-form), as well as the smaller activated forms. The hemopexin domain and the carboxyterminal region are cleaved from the smallest active form of MMP-18, and the RP3MMP18 antibody does not detect these forms. RP3MMP18 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA uses. Collagenase-4 is produced at very low levels in normal, quiescent Xenopus cells and tissues. Collagenase production can be induced by mitogens such as TPA or TNF-a in receptive cell types. Although MMP-18 has been reported in Xenopus tissues, no human orthologue has been identified to date. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Although the sequence homology for this portion of MMP-1 is well conserved, higher concentrations of antibody may be needed for non-human samples

FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS.

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