GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles.
Belongs to the small GTPase superfamily. Arf family.
Detection of ARF1 in Immunoprecipitates of HeLa cell lysate. Antigen-antibody complexes were formed by incubating 500μg of HeLa whole cell lysate with 2μg ab183576 (lane 2) compared with HeLa cell lysate as a positive control (lane 1). For detection, ab183576 was used at 1/1000 dilution.
Immunofluorescent analysis of HeLa cells (formalin-fixed, 0.1% Triton X-100 permeabilized) labeling ARF1 with ab183576 at 1/100 dilution followed with DyLight 488 goat anti-rabbit IgG secondary antibody at 1/400 dilution. Nuclei (blue) were stained with Hoechst 33342 dye.