Description
FAP, also known as Seprase, is a homodimeric integral membrane gelatinase belonging to the serine protease family. FAP includes dipeptidyl peptidase IV (DPPIV/CD26) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. And it's enzymatic activity is dependent on FAP association with DPPIV on the cell surface. The active site of FAP is localized in the extracellular part of the protein and contains a catalytic triad composed of Ser624 Asp702 His734 in humans and mice. It is catalytically active as a 170kD homodimer and has a dipeptidase and an endopeptidase activity. FAP expression is high in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. FAP is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. ecombinant human FAP, fused to His-tag at C-terminus, was expressed in insert cell and purified by using conventional chromatography techniques