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Human FAP Protein 4833

$375.00$1,250.00

Summary

  • Expression: HEK293
  • Active: Yes (catalytic)
  • Amino Acid Range: Leu26-Asp760
SKU: 4833parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

Q12884

express system

HEK293

product tag

N-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Fibroblast activation protein (FAP) is a serine protease that has been reported in fibroblasts and some carcinoma cells, which correlates with poor patient outcomes. FAP can be induced under hypoxia which is also vital in the malignant behaviors of cancer cells.

molecular weight

The protein has a predicted MW of 86.1 kDa. Due to glycosylation, the protein migrates to 90-100 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human FAP Protein 4833

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Fibroblast activation protein (FAP) is a serine protease that has been reported in fibroblasts and some carcinoma cells, which correlates with poor patient outcomes. FAP can be induced under hypoxia which is also vital in the malignant behaviors of cancer cells.
Protein names
Prolyl endopeptidase FAP (EC 3.4.21.26) (170 kDa melanoma membrane-bound gelatinase) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surf
Gene names
FAP,FAP
Protein family
Peptidase S9B family
Mass
9606Da
Function
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. {ECO:0000250|UniProtKB:P97321, ECO:0000269|PubMed:10347120, ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16480718, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:18095711, ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:21288888, ECO:0000269|PubMed:21314817, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413}.
Catalytic activity
BINDING 203; /ligand="substrate"; /evidence="ECO:0000303|PubMed:15809306"; BINDING 204; /ligand="substrate"; /evidence="ECO:0000303|PubMed:15809306"
Subellular location
SUBCELLULAR LOCATION: [Prolyl endopeptidase FAP]: Cell surface {ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7911242}. Cell membrane {ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:9065413}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:2172980}; Single-pass type II membrane protein {ECO:0000255}. Note=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. {ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7911242, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}.; SUBCELLULAR LOCATION: [Antiplasmin-cleaving enzyme FAP, soluble form]: Secreted {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:24371721}. Note=Found in blood plasma and serum. {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:24371721}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000303|PubMed:10644713}.
Tissues
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. {ECO:0000269|PubMed:10347120, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10644713, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:7911242}.
Structure
SUBUNIT: Homodimer; homodimerization is required for activity of both plasma membrane and soluble forms. The monomer is inactive. Heterodimer with DPP4. Interacts with PLAUR; the interaction occurs at the cell surface of invadopodia membranes. Interacts with ITGB1. Interacts with ITGA3. Associates with integrin alpha-3/beta-1; the association occurs in a collagen-dependent manner at the cell surface of invadopodia membranes. {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:15809306, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:9065413}.
Post-translational modification
PTM: N-glycosylated. {ECO:0000269|PubMed:15809306, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:7911242, ECO:0000269|PubMed:9065413}.; PTM: The N-terminus may be blocked.
Target Relevance information above includes information from UniProt accession : Q12884
The UniProt Consortium

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