Human FAP ELISA Kit

Target data

The protein expressed by the FAP gene is a cell surface glycoprotein serine protease involved in the degradation of the extracellular matrix (ECM) and various cellular processes such as tissue remodeling, fibrosis, wound healing, inflammation, and tumor growth. It exists in both plasma membrane-bound and soluble forms, exhibiting post-proline cleaving endopeptidase activity, specifically targeting Ala/Ser-Gly-Pro-Ser/Asn/Ala sequences in substrates like alpha-2-antiplasmin SERPINF2 and SPRY2. FAP protein degrades gelatin and heat-denatured type I collagen but not native type I and IV collagens, nor vitronectin, tenascin, laminin, fibronectin, fibrin, or casein. It also has dipeptidyl peptidase activity, hydrolyzing prolyl bonds when the penultimate residue is proline, with a preference for sequences such as Ala-Pro and Gly-Pro. It acts on natural neuropeptides like neuropeptide Y, peptide YY, substance P, and brain natriuretic peptide 32. In its membrane form, in association with DPP4, PLAUR, or integrins, FAP is involved in pericellular ECM proteolysis, promoting cell adhesion, migration, invasion, and plays roles in development, wound healing, and cell invasiveness in malignant melanoma. It supports tumor progression by facilitating angiogenesis, collagen degradation, apoptosis, and reducing immune response. Additionally, it promotes glioma cell invasion by degrading brevican and functions as a tumor suppressor in melanocytic cells by regulating cell proliferation and survival independently of its serine protease activity. This supplementary information is collated from multiple sources and compiled automatically.