FAP

GeneName

FAP

Summary

FAP, also known as fibroblast activation protein alpha or seprase, is an 88 kDa type II transmembrane serine protease expressed on the surface of activated fibroblasts, particularly in the tumour microenvironment. It is involved in various cellular processes, including cell adhesion, migration, and proteolysis, and is localised to the plasma membrane, extracellular space, and cytoplasm. FAP plays a role in the regulation of extracellular matrix dynamics and is implicated in angiogenesis and apoptosis, functioning through its endopeptidase activity and interactions with integrins and other proteins.

Importance

FAP is relevant to: - Cancer research, as it is overexpressed in many tumours and contributes to tumour progression and metastasis - Tissue remodelling and fibrosis, given its role in extracellular matrix regulation - Potential therapeutic targeting in fibroblast activation and related pathologies - Understanding immune responses and inflammation, as it influences fibroblast behaviour in various contexts

Top Products

For researchers investigating FAP, we recommend two excellent primary antibodies that cater to various experimental needs. The first is the well-cited polyclonal antibody, Anti-Fibroblast activation protein, alpha antibody (ab53066), which has garnered 155 citations, highlighting its reliability in the field. This antibody is particularly effective for immunohistochemistry (IHC) and western blotting (WB), making it a solid choice for those requiring robust detection methods.In addition, we offer the recombinant antibody, Anti-Fibroblast activation protein, alpha antibody [EPR20021] (ab207178). This monoclonal antibody has also been validated for IHC and WB, and it boasts 144 citations, demonstrating its strong presence in research. The recombinant nature of this product ensures batch-to-batch consistency, making it an ideal option for researchers seeking dependable results in their studies of FAP. "The Human FAP ELISA Kit (ab256404) is a reliable option for researchers looking to measure FAP levels in their samples."

Abcam Product Citation Summary

The data indicates that FAP antibodies are widely used in various applications, including western blotting, immunohistochemistry, and immunofluorescence, across different human and mouse tissues. The studies focus on significant medical contexts such as cancer, atherosclerosis, and rheumatoid arthritis, highlighting the relevance of FAP in these conditions.

Abcam Product Citation Table

Function

Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16410248, PubMed:16480718, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711, PubMed:2172980, PubMed:7923219, PubMed:9065413). Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16410248, PubMed:16651416, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). 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. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. 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 activity-independent manner.

Post-translational modifications

N-glycosylated.

The N-terminus may be blocked.

Sequence Similarities

Belongs to the peptidase S9B family.

Tissue Specificity

Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from inflamed synovial tissues. Expressed in activated hepatic stellate cells (HSC) and myofibroblasts from cirrhotic liver, but not detected in normal liver. Expressed in glioma cells (at protein level). Expressed in glioblastomas and glioma cells. Isoform 1 and isoform 2 are expressed in melanoma, carcinoma and fibroblast cell lines.

Cellular localization

• Prolyl endopeptidase FAP
• Cell surface
• Cell membrane
• Single-pass type II membrane protein
• Cell projection
• Lamellipodium membrane
• Single-pass type II membrane protein
• Cell projection
• Invadopodium membrane
• Single-pass type II membrane protein
• Cell projection
• Ruffle membrane
• Single-pass type II membrane protein
• Membrane
• Single-pass type II membrane protein
• Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin.
• Antiplasmin-cleaving enzyme FAP, soluble form
• Secreted
• Found in blood plasma and serum.
• Isoform 2
• Cytoplasm

Alternative names

Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, FAPalpha, SIMP, Seprase, FAP

Database links

swissprot:Q12884 entrezGene:2191 omim:600403

Other research areas

• Oncology