|Other Names||ADP-ribosylation factor-like protein 4C, ADP-ribosylation factor-like protein 7, ADP-ribosylation factor-like protein LAK, ARL4C, ARL7|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2310a was selected from the N-term region of human ARL7 . 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||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). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. May be involved in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in the GDP-bound form. Regulates the microtubule-dependent intracellular vesicular transport from early endosome to recycling endosome process.|
|Cellular Location||Cell projection, filopodium. Cell membrane. Cytoplasm|
|Tissue Location||Expressed in several tumor cell lines (at protein level). Expressed in lung, brain, leukocytes and placenta|
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Provided below are standard protocols that you may find useful for product applications.
ADP-ribosylation factor-like 7 is a member of the ADP-ribosylation factor family of GTP-binding proteins. ARL7 is closely similar to ARL4 and ARL6 and each has a nuclear localization signal and an unusually high guanine nucleotide exchange rate.
Jacobs, S., et al., FEBS Lett. 456(3):384-388 (1999).
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