MMP-10 (Stromelysin-2, Transin-2) is a close relative (78% identical) to MMP-3 (Stromelysin-1), and as such shares much of the same properties as this enzyme. The 476 amino acid human MMP-10 has a predicted mass of 54.2 kDa, and apparent mass of 56 kDa on reduced SDS PAGE gels. The predicted pI is 5.37, similar to the 5.7 pI of human MMP-3, although rat MMP-10 is more basic at 6.22 pI. MMP-10 cleaves collagen types III, IV and V, fibronectin, gelatin, aggrecan and proteoglycans. Both MMP-3 and MMP-10 digest casein in zymograms, and are difficult to quantify independently by that method. The biggest differences in MMP-10 and MMP-3 are a lack of glycosylation in MMP-10, and differential expression. Keratinocytes produce MMP-10, and fibroblasts MMP-3, although many tumors and corneas from diabetic patients produce both MMP-3 and MMP-10. Because of the similarities between MMP-3 and MMP-10, specific antibodies are difficult to make. RP1-MMP-10 recognizes both MMP-10 and MMP-3, and a companion antibody, RP2MMP-10, recognizes only MMP-10. RP1-MMP-10 anti-MMP-10 works well for Western blotting applications, and when used against the reduced protein identifies bands at 56 kDa (the pro-form), as well as the initial active forms (46 kDa). The propeptide domain is enzymatically removed during activation of MMP-10, and the RP1MMP-10 antibody only recognizes the latent MMP-10. RP1-MMP-10 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA uses. Stromelysin-2 is produced at very low levels in normal, quiescent cells and tissues. Stromelysin-2 production can be induced by mitogens such as TPA or TNF-_ in receptive cell types. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Although the sequence homology for this portion of MMP-10 is well conserved, higher concentrations of antibody may be needed for non-human samples.

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