Human seprase ELISA kit for the quantitative detection of human seprase in cell culture supernates, serum and plasma (heparin, EDTA).

FAP (fibroblast activation protein-alpha) also known as FAPA or seprase, is an inducible cell surface glycoprotein that was originally identified in cultured fibroblasts using monoclonal antibody F19. The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. The FAP gene is mapped on 2q24.2. FAP is most closely related to DPPIV and they share about 50% of their amino acids. FAP is catalytically active as a 170kD dimer and has dipeptidase and gelatinase activity. Its gelatinase activity requires a glycine in P2 position. FAP-alpha shows 48% amino acid identity with dipeptidyl peptidase IV and 30% identity with DPP4-related protein. Northern blot analysis detected a 2.8-kb FAP-alpha mRNA in fibroblasts. Depletion of FAP-expressing cells, which made up only 2% of all tumour cells in established Lewis lung carcinomas, caused rapid hypoxic necrosis of both cancer and stromal cells in immunogenic tumors by a process involving interferon-gamma and tumour necrosis factor-alpha.