The image on the left is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using CSB-PA957575(ARF1 Antibody) at dilution 1/25, on the right is treated with synthetic peptide. (Original magnification: ×200)
Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Human fetal brain tissue, Human kidney tissue, Primary antibody: CSB-PA957575(ARF1 Antibody) at dilution 1/500, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 1 minute
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2 and ARF3), class II (ARF4 and ARF5) and class III (ARF6), and members of each class share a common gene organization. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.
-20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol
Antigen affinity purification
ADP-ribosylation factor 1
Homo sapiens (Human)
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
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).