Adenosine diphosphate ribosylation factor 1 (ARF1) protein belongs to the class I ARF family of proteins. This protein is present in the Golgi apparatus. The ARF1 gene is located on the human chromosome at 1q42.13.
Immunogen
Synthetic peptide directed towards the middle region of human ARF1
Application
Anti-ARF1 antibody produced in rabbit has been used in western blotting.[1]
Biochem/physiol Actions
Adenosine diphosphate ribosylation factor 1 (ARF1) plays a role in mediating retrograde and anterograde vesicular traffic. This protein also plays a role in the synthesis of coat protein I (COP-I) coated vesicles. ARF1 is involved in the recruitment of clathrin adaptor complexes such as activator protein 1, 3, and 4. The activation of ARF1 triggers the assembly of spectrin as well as actin cytoskeleton in the Golgi membranes.
Sequence
Synthetic peptide located within the following region: MRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQA
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
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The Journal of biological chemistry, 287(6), 3885-3897 (2011-12-14)
ADP-ribosylation factor 1 (Arf1) plays a major role in mediating vesicular transport. Brefeldin A (BFA), a known inhibitor of the Arf1-guanine nucleotide exchange factor (GEF) interaction, is highly cytotoxic. Therefore, interaction of Arf1 with ArfGEF is an attractive target for
Transcriptional features of multiple myeloma patients with chromosome 1q gain.
The small GTPase ADP-ribosylation factor-1 (Arf1) plays a key role in the formation of coat protein I (COP I)-coated vesicles. Upon recruitment to the donor Golgi membrane by interaction with dimeric p24 proteins, Arf1's GDP is exchanged for GTP. Arf1-GTP
The ADP-ribosylation factor (ARF) small GTPases regulate vesicular traffic and organelle structure by recruiting coat proteins, regulating phospholipid metabolism and modulating the structure of actin at membrane surfaces. Recent advances in our understanding of the signalling pathways that are regulated
Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotide-binding (G) proteins, including the ARF-like (ARL) proteins and SAR1, regulate membrane traffic and organelle structure by recruiting cargo-sorting coat proteins, modulating membrane lipid composition, and interacting with regulators of other G
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