Anti-ARF1, clone 1A9/5

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. The ADP-ribosylation factor (ARF) family comprises a group of structurally and functionally conserved proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. The ARF family is divided functionally into the ARF and the ARF-like proteins. ARF s share more than 60% sequence identity, appear to be ubiquitous in eukaryotes, and are highly conserved evolutionarily. ARF is involved in intracellular protein traffic to and within the Golgi complex. ARF has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. Protein function: 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. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity, the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD). [The UniProt Consortium]