Fibroblast activation protein (FAP) is a type II transmembrane serine protease and a cell surface antigen. It is present as a homodimeric integral protein with dipeptidyl peptidase IV like fold. FAP has an α/β-hydrolase domain and an eight-bladed β-propeller domain. It is not expressed in normal tissues. The protein is only expressed by activated fibroblasts in response to pathologic situations.
Immunogen
Synthetic 18 amino acid peptide from extracellular domain of human FAP. Percent identity with other species by BLAST analysis: Human, Gorilla, Gibbon (100%); Monkey (94%); Bovine (89%); Marmoset (83%).
Application
Anti-FAP (AB1) antibody produced in rabbit has been used in immunohistochemistry.
Biochem/physiol Actions
Fibroblast activation protein (FAP) is expressed in several pathogenic sites including cancer, fibrosis, arthritis, wounding, or inflammation. FAP has in vitro dipeptidyl peptidase activity and collagenolytic activity. It cleaves N-terminal dipeptides from polypeptides and can degrade gelatin and type I collagen.
Features and Benefits
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Physical form
Solution in phosphate-buffered saline containing less than 0.1% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Cancer-associated fibroblasts (CAF) are components of the tumor microenvironment whose contributions to malignant progression are not fully understood. Here, we show that the fibroblast activation protein (FAP) triggers induction of a CAF subset with an inflammatory phenotype directed by STAT3
Pancreatic ductal adenocarcinoma (PDAC) is projected to become the second leading cause of cancer-related death. Hallmarks include desmoplasia with variable extracellular matrix (ECM) architecture and a complex microenvironment with spatially defined tumor, stromal, and immune populations. Nevertheless, the role of
Clinical and experimental immunology, 184(3), 265-283 (2015-12-17)
Dipeptidyl peptidase (DPP) 4 (CD26, DPP4) is a multi-functional protein involved in T cell activation by co-stimulation via its association with adenosine deaminase (ADA), caveolin-1, CARMA-1, CD45, mannose-6-phosphate/insulin growth factor-II receptor (M6P/IGFII-R) and C-X-C motif receptor 4 (CXC-R4). The proline-specific
FAP Promotes Immunosuppression by Cancer-Associated Fibroblasts in the Tumor Microenvironment via STAT3?CCL2 Signaling
Xuguang Yang
Cancer Research (2016)
Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha
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