|Other Names||ADP-ribosylation factor-like protein 1, ARL1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2304c was selected from the C-term region of human ARL1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||GTP-binding protein that recruits several effectors, such as golgins, arfaptins and Arf-GEFs to the trans-Golgi network, and modulates their functions at the Golgi complex (PubMed:9624189, PubMed:21239483, PubMed:27436755, PubMed:22679020, PubMed:27373159). Plays thereby a role in a wide range of fundamental cellular processes, including cell polarity, innate immunity, or protein secretion mediated by arfaptins, which were shown to play a role in maintaining insulin secretion from pancreatic beta cells (PubMed:22981988).|
|Cellular Location||Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane. Membrane; Lipid-anchor|
|Tissue Location||Detected in heart, liver, lung and liver (at protein level). Detected in fetal heart, lung, liver and kidney Detected in adult heart, placenta, lung, liver, skeletal muscle, kidney and pancreas.|
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Provided below are standard protocols that you may find useful for product applications.
ARL1 belongs to the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally related to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, regulate intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform. Although, ARL proteins were initially thought not to activate CT or PLD, later work showed that they are weak stimulators of PLD and CT in a phospholipid dependent manner.
Hong, J.X., et al., J. Biol. Chem. 273(25):15872-15876 (1998).Zhang, G.F., et al., J. Biol. Chem. 270(1):21-24 (1995).
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