|Application ||WB, E|
|Calculated MW||43923 Da|
|Antigen Region||280-310 aa|
|Other Names||Ecto-ADP-ribosyltransferase 3, ADP-ribosyltransferase C2 and C3 toxin-like 3, ARTC3, Mono(ADP-ribosyl)transferase 3, NAD(P)(+)--arginine ADP-ribosyltransferase 3, ART3, TMART|
|Target/Specificity||This ART3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 280-310 amino acids from the C-terminal region of human ART3.|
|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||ART3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Cellular Location||Cell membrane; Lipid-anchor, GPI-anchor.|
|Tissue Location||Testis specific.|
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Provided below are standard protocols that you may find useful for product applications.
Mono-ADP-ribosylation involves the transfer of the ADP-ribose moiety from NAD+ to a specific amino acid in the target protein. The rodent mono-ADP-ribosyltransferase RT6 is a glycosylphosphatidylinositol (GPI)-anchored membrane protein specifically expressed at the cell surface of rat and mouse T lymphocytes. The predicted 367-amino acid human ART3 protein has an estimated molecular mass of 41.5 kD and contains a hydrophobic peptide signal at its N terminus, 3 consensus motifs specific to enzymes catalyzing ADP-ribose transfer, a hydrophobic C-terminal sequence characteristic of a GPI-anchored protein, a novel motif repeated 3 times at its C terminus, and 1 potential glycosylation site.1 The ART3 and rodent RT6 proteins share 35% amino acid identity.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).
Koch-Nolte, F., et al., Genomics 39(3):370-376 (1997).
Levy, I., et al., FEBS Lett. 382(3):276-280 (1996).
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