- CITATIONS: 2
|Application ||WB, IHC-P, E|
|Calculated MW||44668 Da|
|Antigen Region||377-406 aa|
|Other Names||ADP-ribosylation factor GTPase-activating protein 1, ARF GAP 1, ADP-ribosylation factor 1 GTPase-activating protein, ARF1 GAP, ARF1-directed GTPase-activating protein, ARFGAP1, ARF1GAP|
|Target/Specificity||This ARFGAP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 377-406 amino acids from the C-terminal region of human ARFGAP1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||ARFGAP1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity).|
|Cellular Location||Cytoplasm. Golgi apparatus. Note=Associates with the Golgi complex|
Provided below are standard protocols that you may find useful for product applications.
ARFGAP1 is a GTPase-activating protein (GAP) which associates with the Golgi apparatus and which interacts with ADP-ribosylation factor 1 (ARF1). The encoded protein promotes hydrolysis of ARF1-bound GTP and is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. The activity of this protein is stimulated by phosphoinosides and inhibited by phosphatidylcholine.
Huber, I., et al., Meth. Enzymol. 329, 307-316 (2001).
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