MT3MMP was identified as a membrane-bound Metalloproteinase in normal and tumor cell lines. MMP-16 is similar to the other Mt-MMPs; it contains a furin cleavage site, is membrane bound, and contains a cytoplasmic tail (MT4MMP lacks the tail, and is thought to be GPI anchored to the cell surface). MT3MMP is also known to be "shed" from the membrane in a soluble form. MT1MMP is known to function in activating a number of MMPs, chiefly MMP-2, but that role has not been well described for the other MTMMPs. RP2MMP16 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 65 Kd and 63 Kd (the pro-form and active form), as well as activation/breakdown products. The antibody can recognize native or reduced MT3MMP, and has application for Western blotting, but the Cytoplasmic tail is not accessible to the cell surface, thus the cells or tissue needs to be permeabilized for the antibody to gain access to the epitope. MT3MMP has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin-A or the phorbol ester TPA stimulates production of MT3MMP in some cell types, and the enzyme can be recovered in cell lysates. A recommended starting concentration for Western blots is 1:2,000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentration of antibody may be needed for non-human samples

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