Matriptase-2, also known as MTSP-2 (membrane-type serine proteinase-2), TMSP6 (Type-II Membrane Serine Proteinase-6) and PVAE354, is a type-II serine proteinase. Matriptase-2 shares approximately 37% identity with matriptase-1 and matriptase-3, mostly in the catalytic domain. Matriptase-2 is an S1A family proteinase, in the PA clan of serine proteinases, which includes trypsin, chymotrypsin, acrosin, and many other key enzymes. A literature alias exists for MTSP-2, the Mouse Serine-Type Proteinase, granzyme-A. Matriptase-2 is organized by an aminoterminal cytoplasmic domain, followed by a transmembrane domain, a stem region and then two CUB domains, three LDL receptor-like motifs, and a carboxyterminal catalytic domain. The full-length human matriptase-2 is an 802 amino acid protein with predicted (unmodified) mass of 88.9 kDa, and a pI of 6.04. Secreted Matriptase-2 is glycosylated, and runs at approximately 95 kDa on reduced SDS-PAGE gels. Like matriptase-1, matriptase-2 is shed from the membrane by a cleavage in the stem region, and the catalytic domain can be cleaved from the regulatory domains to generate a free trypsin-like enzyme. The free enzyme is not detected by RP2Matriptase-2. Matriptase-2 may be more limited in distribution than matriptase-1, and has been identified in the liver by message, but appears to be in kidney, liver and uterus, and in a number of cell lines. 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. Higher concentrations of antibody may be needed for samples from more distantly related species. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen.

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