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).
Applications:Suitable for use in ELISA.
Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:Store product at 4°C if to be used immediately within two weeks.
For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C.
Aliquots are stable at -20°C for 12 months after receipt.
Dilute required amount only prior to immediate use.
Further dilutions can be made in assay buffer.
Note: Sodium azide is a potent inhibitor of peroxidase and should not be added to HRP conjugates.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size:50ug
Host:rabbit
Source Antibody:human
Grade:Affinity Purified
Purity:Purified by Protein G affinity chromatography.
Form:Supplied as a liquid in 0.01M PBS, pH 7.4, 0.03% Proclin 300, 50% glycerol. Labeled with horseradish peroxidase (HRP).
Specificity:Recognizes human ARF1.
Isotype:IgG
Calc Applications Abbrev:E
Calc Crossreactivity:Hu
Immunogen:Recombinant protein corresponding to aa2-181 from human ADP-ribosylation factor 1.