FAP-1 (Tyrosine-protein Phosphatase Non-receptor Type 13, Fas-associated Protein-tyrosine Phosphatase 1, PTP-BAS, Protein-tyrosine Phosphatase 1E, PTP-E1, hPTPE1, Protein-tyrosine Phosphatase PTPL1, PTPN13, PNP1, PTP1E, PTPL1)

FAP-1 (also known as Fas-associated phosphatase-1, PTPN13, PTP-BAS, hPTPIE, and PTPL1) is a member of the protein tyrosine phosphatase (PTP) family. PTPs are enzymes that catalyze the removal of a phosphate group attached to a tyrosine residue. Most intracellular signaling involves reversible phosphorylation events; therefore, PTPs are central to the dynamic regulation of signaling cascades that underlie cell functions. For example, PTPs play key roles in regulating cell growth, differentiation, proliferation, inflammation, and oncogenic transformation. PTPs are emerging as a promising class of signaling targets for diseases such as cancer, neurodegeneration, diabetes, and inflammation. A key challenge is to identify specific PTPs that are invovled in a disease process and develop therapeutics to modulate the PTP. FAP-1 phosphatase is thought to be important in the Fas signaling pathway. FAP-1 binds to the cytosolic tail of the Fas receptor (Apo1, CD95) and inhibits Fas-induced apoptosis. Increased FAP-1 protein levels in some tumor cell lines and tumor tissues correlates with resistance to Fas-mediated apoptosis. In general, FAP-1 expression has been found to be highest in cell lines and tissues that are relatively resistant to Fas-mediated apoptosis. Gene transfer-mediated elevations in FAP-1 partially abolished Fas-induced apoptosis in a T cell line which is consistent with an inhibitory effect of FAP-1 on Fas signal transductions. Additionally, FAP-1 expression correlates with Fas resistant in ovarian cancer cell lines and FAP-1 is commonly expression in ovarian cancers. Human Fas has a putative consensus tyrosine phosphorylation site (Tyrosine 275) suggesting that Fas surface expression or signaling may be regulated by phosphorylation. FAP-1 has been shown to directly bind to Fas and may dephosphorylate Fas as part of the down regulation of the apoptotic pathway. It is thought that development of therapeutics to inhibit FAP-1 may increase the ability of tumor cells with upregulated FAP-1 to undergo apoptosis. FAP-1 is a large ~270kD protein. Multiple alternatively spliced FAP-1 transcript variants which encode distinct proteins have been reported, including shorter forms. Please see Application Notes section for additional details on FAP-1 isoforms. Recognizes FAP-1, including FAP-1 isoforms listed in the Application Notes section.\n\nApplications:\nSuitable for use in Western Blot, Immunohistochemistry, Immunofluorescence, Immunocytochemistry and Immunoprecipitation. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: 1:1000-1:2000\nImmunohistochemistry (formalin fixed paraffin embedded): 1:1000-1:5000\nImmunoprecipitation: 1:50-1:200\nImmunohistochemistry: Frozen\nImmunofluorescence: 1:500-1:3000\nImmunocytochemistry: 1:500-1:3000\nOptimal dilutions to be determined by the researcher.\n\nPositive Control: \nSpleen, lymphoid, many cancer cell lines\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

F0019-53N3

Size

50ul

Applications

ICC, IF, IHC, IP, WB

Hosts

Rabbit

Reactivities

Hum

Form

Supplied as a liquid, 0.05% sodium azide.

P Type

Pab

Purity

Serum

Isotype

IgG

References

1. Sakaskan E, R Ravid, F Meier, F Muller-Spahn, and R Jockers. 2005. Immunohistochemical localization of Fas-associated phosphatase-1 (FAP-1) in Alzheimer Disease hippocampus. Appl Immunohistochem Mol Morphol 13:190-193. 2. Foehr ED, G Lorente, V Vincent, K Nikolich, and R Urfer. 2005. FAS associated phosphatase (FAP-1) blocks apoptosis of astrocytomas through dephosphorylation of FAS. J Neuro-Oncology. 74:241-248. 3. Ivanov VN, Z Ronai, and TK Hei. 2005. Opposite roles of FAP-1 and dynamin in the regulation of Fas (CD95) translocation ot the cell surface and susceptibility to Fas ligand-mediated apoptosis. J Biol Chem. 281:1840-1852.

Additional Info

Recognizes human FAP-1.