ADP-ribosylation represents a posttranslational modification that involves transfer of ADP-ribose moiety from NAD+ to a specific amino acid in target protein (greatly modifying protein function) with the release of nicotinamide moiety. It was originally discovered as a mechanism by which potent bacterial toxins, such as Diphtheria toxin and Cholera toxin, modify and inactivate human target proteins, and these toxins were suggested to mimic mammalian endogenous ADP-ribosyltransferases. ART2 is an ecto-ADP-ribosyltransferases family (ART1-ART5) member which distantly resembles ADP-ribosylating bacterial toxins. It is expressed by mature T cells in which it ADP-ribosylates the integrin LFA-1 as well as other cell surface proteins, and this ART2-mediated ADP-ribosylation of T cell surface proteins provides a novel means for triggering T cell apoptosis. Ethenoadenosine moiety is contained in NAD analogue etheno-NAD which serves as an efficient substrate for ADP-ribosyltransferases and ethenoadenosine specific antibody clone 1G4 can be used for detection of ADP-ribosylated amino acids (ADP-ribosylation of cellular proteins) by FACS/FLOW, ICC-IF and Western blot applications.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
Publications for Ethenoadenosine Antibody (NB600-442)(15)
We have publications tested in 4 confirmed species: Human, Mouse, Rat, Chicken.
We have publications tested in 3 applications: FLOW, ICC/IF, WB.