Use

MMP-11, first described as a tumor-specific MMP, was later found to be produced by a wide variety of cell types under different conditions. The sequence for MMP-11 is most similar to MMP-3, but MMP-11 seems to either have a much more restricted substrate specificity or much lower activity than MMP-3 (Stromelysin-1). In addition, MMP-11 contains a furin-cleavage site that MMP-3 lacks. MMP-11 has been detected in a number of cell types, including dermal fibroblasts, lung fibroblasts and many tumor cell lines. MMP-11 is secreted in a glycosylated form, and the zymogen is found at about 64 kd. The enzyme is rapidly activated to a 58 kd form, a 45-47 kd size, then to a 28 kd final active form. Depending on the activation method, the MMP-11 can be seen as a cascade of active forms. RP4MMP11 Anti-MMP-11 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 58 Kd (the zymogen), but not the activated forms at 45 Kd, and a series of further cleaved active forms. RP4MMP11 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. MMP-11 is not constituitively produced by most cell types; it has been found in lung fibroblasts, and gingival fibroblasts when stimulated with EGF, as well as breast tumor and osteosarcoma cell lines. Cell types differ greatly in the quantity of MMP-11 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.

FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS.

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