Fibroblast activation protein (FAP), a cell-surface type II transmembrane glycoprotein serine protease, has a cytoplasmic tail, a single transmembrane domain, and an extracellular domain. It is a member of the S9b family of post-proline cleaving enzymes. FAP is localized in the plasma membrane. FAP gene is mapped to human chromosome 2q24.2. Expression of FAP is hardly seen in adult tissues.
Immunogen
FAP (AAH26250, 525 a.a. ~ 624 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Monoclonal Anti-FAP antibody produced in mouse has been used in western blotting.[1]
Biochem/physiol Actions
Fibroblast activation protein (FAP) participates in the remodeling of tissue, wound healing, inflammation, fibrosis, and tumor development. It possesses dipeptidyl peptidase and endopeptidase activities. FAP plays a key role in the remodeling of extracellular matrix structure and the reconstruction of tumor microarray. Overexpression of the FAP gene might return epithelial ovarian cancer after chemotherapy. FAP gene expression is involved in cancer cells and premalignant metaplastic cells of the esophagus.
Physical form
Solution in phosphate buffered saline, pH 7.4
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