|Other Names||ADP-ribosylation factor-like protein 3, ARL3, ARFL3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2306a was selected from the N-term region of human ARL3 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|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||Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Requires assistance from GTPase- activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium. Does not act as an allosteric activator of the cholera toxin catalytic subunit.|
|Cellular Location||Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Cell projection, cilium Note=Detected predominantly in the photoreceptor connecting cilium. Present on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules|
|Tissue Location||Expressed in the retina. Strongly expressed in connecting cilium, the myoid region of the inner segments (IS) and in cone photoreceptors (at protein level)|
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ADP-ribosylation factors (ARFs) are low molecular weight GTP-binding proteins belonging to the RAS superfamily. The predicted 182-amino acid ARL3 (ADP-ribosylation like factor) protein shares 97% amino acid identity with rat ARLl3 and 43% identity with human ARF1. Like the ARFs, ARL3 has a glycine at position 2, the site of N myristoylation, and lacks cysteine residues near the C terminus, which are found in other members of the RAS family. Northern blot analysis detected a 1-kb ARL3 transcript in all tissues tested, with highest expression in heart and lung, and lower expression in brain, liver, kidney, ovary, and testis. A 5.5-kb transcript was also detected in most tissues, with highest expression in brain. Immunoblot analysis detected ARL3 in human tumor cell lines but not in normal rodent cells. Although ARL3 binds GTP, it is devoid of activity in the cholera toxin-dependent ADP-ribosylation of Gs, and is therefore classified as an ARF-like protein.
Cavenagh, M.M., et al., J. Biol. Chem. 269(29):18937-18942 (1994).Adams, M.D., et al., Nature 377 (6547 Suppl), 3-174 (1995).Kim, H.S., Cytogenet. Cell Genet. 83 (3-4), 246 (1998).Wistow, G., et al., Mol. Vis. 8, 196-204 (2002).
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