FAP (also known as seprase) is a Type II transmembrane serine protease. Both plasma membrane and soluble forms exhibit postproline cleaving endopeptidase activity, with a marked preference for Ala/SerGlyProSer/Asn/Ala consensus sequences. Degrade also gelatin, heatdenatured type I collagen. Also has dipeptidyl peptidase activity, with a preference for AlaPro, IlePro, GlyPro, ArgPro and ProPro. The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activityindependent manner. - Proteine/Peptide
Immobilized Anti-FAP Antibody, Mouse IgG2a (FAP5) at 1 µg/mL (100 µL/well) can bind FITC-Labeled Human FAP, Fc Tag (Cat. No. FAP-HF263) with a linear range of 0.02-0.313 µg/mL (QC tested).
FAP-HF263-200ug
FITC-Labeled Human FAP, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
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