Fibroblast activation protein α (FAP), also known as seprase, is a type II transmembrane serine protease that can be shedded into plasma. FAP is a proline specific enzyme with a preference of Proline as P1 residue. FAP and a dipeptidyl peptidase 4 (DPP4) shares similar structural fold, featuring an α/β-hydrolase domain and an eight bladed β-propeller domain. Known DPP4 dipeptides are cleaved by FAP with an 100- fold decrease in catalytic efficiency compared with DPP4. In addition to dipeptidyl peptidase activity, it possesses endopeptidase activity capable of cleaving gelatin and type I collagen. FAP is expressed in the majority of epithelial cancer-associated fibroblasts, in granulation tissue of healing wounds, and in bone and soft tissue sarcomas. Expression of FAP is not detected in fibroblasts of benign epithelial tumors or normal adult tissues. It has been implicated in tumor growth and metastasis, and in extracellular matrix remodeling. The shedded FAP in plasma can cleave α-2-antiplasmin (Serpin F2) into a more active form.
Size
25 μg
Concentration
n/a
Applications
BA
Other Names
FAP, FAP-alpha, Fibroblast Activation Protein alpha, fibroblast activation protein, alpha, Integral membrane serine protease, Seprase, DPP4