Background: ADP-ribosylation factors, or ARFs, enhance the ADP ribosyltransferase activity of cholera toxin and are implicated in vesicle transport between endoplasmic reticulum and the Golgi complex. Arfaptin 1 is recruited from the cytosol to Golgi membranes by ARFs in a guanosine 5-prime-O-(3-thiotriphosphate)-dependent and brefeldin A-sensitive manner but is not a constituent of coatomer. Arfaptin 1 binds to nonmyristoylated GTP-bound ARF3, but not to GDP-bound ARF3, and also to ARF1, another class I ARF. It binds with lower affinity to ARF5, a class II ARF, and with very little affinity to ARF6, a class III ARF. POR1 (also designated Arfaptin 2) was first isolated as a Rac 1 binding protein necessary for Rac mediated actin polymerization and the subsequent formation of membrane ruffles and lamellipodia. POR1 has also been shown to interact with the ADP ribosylation factor ARF6, a GTPase that associates with the plasma membrane and intracellular endosome vesicles, in a GTP dependent manner. The association of POR1 with ARF6 stimulates induction of actin polymerization. POR1 appears to play a regulatory role through multiple signaling pathways in the reorganization of the cytoskeletal structure.
Description: Rabbit polyclonal to Arfaptin 1
Immunogen: KLH conjugated synthetic peptide derived from Arfaptin 1
Specificity: ·Reacts with Human, Mouse, Pig, Dog and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 44 kDa;
·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;
·Immunocytochemistry/Immunofluorescence: 1/100;
·Immunoprecipitation: 1/50;
·ELISA: 1/500;
·Optimal working dilutions must be determined by the end user.
