Anti poly mono adp ribose

Manufactured by Cell Signaling Technology

Sourced in United States, United Kingdom

Anti-poly/mono-ADP-ribose is a laboratory reagent that detects the presence of poly(ADP-ribose) or mono(ADP-ribose) in biological samples. It functions by binding to and labeling these ADP-ribose modifications.

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Lab products found in correlation

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Poly/mono-ADP ribose (5 citations)

4 protocols using anti poly mono adp ribose

Antibody Generation and Verification

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The following antibodies were purchased: anti-Flag (MBL, M185-3L), anti-HA (MBL, M180-3), anti-VAPB (Proteintech, 14477-1-AP and 66191-1-Ig), anti-SCRN1 (Proteintech, 14303-1-AP), anti-GAPDH (Proteintech, 60004-1-Ig and 10494-1-AP), anti-poly/mono-ADP-ribose (Cell Signaling Technology, 83732S), PAR/pADPr (R&D Systems, 4335-MC-100), anti-Calnexin (Novus, NB300-518), anti-His (Proteintech, 66005-1-Ig), anti-GST (Proteintech, 66001-2-Ig), DyLight 488-conjugated goat anti-mouse IgG (Abbkine, A23210), Dylight 594-conjugated goat anti-rabbit IgG (Abbkine, A23420), horseradish peroxidase (HRP)-conjugated mouse anti-rabbit IgG LCS (Abbkine, A25022), HRP-conjugated goat anti-mouse IgG (Proteintech, 15014), and HRP-conjugated goat anti-rabbit IgG (Proteintech, 15015).
Antibodies against ARTC1, ARTC3, ARTC4, and ARTC5 were generated by immunizing rabbits with recombinant proteins GST-ARTC1 (N23–C295), GST-ARTC3 (N27–C362), GST-ARTC4 (N47–C285), and GST-ARTC5 (N23–C291), respectively, purified in our laboratory. Serum samples were obtained from immunized rabbits and incubated with AminoLink Plus Coupling Resin (Thermo, 20501) in Pierce Disposable Plastic Columns (Thermo, 29922). The resin was washed three times with PBS. Antibodies were eluted by 100 mM Glycine (pH 2.5).

Ma X., Li M., Liu Y., Zhang X., Yang X., Wang Y., Li Y., Wang J., Liu X., Yan Z., Yu X, & Wu C. (2023). ARTC1-mediated VAPB ADP-ribosylation regulates calcium homeostasis. Journal of Molecular Cell Biology, 15(7), mjad043.

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Antibody Validation for Cell Signaling

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Sulforhodamine B, tunicamycin, and GSH-EE were purchased from Sigma‒Aldrich (St. Louis, MO, USA). A genomic DNA kit was obtained from Promega (Madison, WI, USA). The anti-β-Tubulin (#2128), anti-ATF3 (#18665), anti-GADD45A (#4632), anti-ATF6 (#65880), anti-CHOP (#2895), anti-GRP78 (#3177), anti-XBP1 (#40435), anti-IRE1α (#3294), anti-DR5 (#8074), anti-Bax (#2772), anti-ATF4 (#11815), anti-Puma (#4976), anti-PERK (#3192), anti-p-eIF2α (#9721), anti-eIF2α (#9722), anti-p-JNK (#9251), anti-JNK (#9252), anti-cytochrome c (#4272), anti-COXIV (#4850), anti-Calnexin (#2679), anti-PARP1 (#9542), anti-Poly/Mono-ADP Ribose (#83732), anti-Caspase 3 (#9662), anti-Caspase 8 (#9746), and anti-Caspase 9 (#9502) antibodies were obtained from Cell Signaling Technology (Beverly, MA, USA). The anti-PARP16 antibody (ab154510) was obtained from Abcam (Cambridge, UK), the anti-Sestrin2 antibody (10795-1-AP) was obtained from Proteintech (Rosemont, IL, USA), the anti-CYB5R3 antibody (BS-12162R) was obtained from Bioss Antibodies Inc. (Woburn, MA, USA), the anti-GAPDH antibody (LF-P-A0212) was obtained from AbFrontier (Seoul, Korea), the anti-ARTC1 (SAB1300652) and anti-Flag (F1804) antibodies were obtained from Sigma‒Aldrich, and the mouse anti-FITC (sc-2010) and rabbit anti-rhodamine (sc-2492) antibodies were obtained from Santa Cruz Biotechnology (Dallas, TX, USA).

Im J.Y., Kim S.J., Park J.L., Han T.H., Kim W.I., Kim I., Ko B., Chun S.Y., Kang M.J., Kim B.K., Jeon S.A., Kim S.K., Ryu I., Kim S.Y., Nam K.H., Hwang I., Ban H.S, & Won M. (2024). CYB5R3 functions as a tumor suppressor by inducing ER stress-mediated apoptosis in lung cancer cells via the PERK-ATF4 and IRE1α-JNK pathways. Experimental & Molecular Medicine, 56(1), 235-249.

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Characterizing PARP7 Interactions with NF-κB

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Cos-1 cells were transfected with 0.5 µg of p50 cFlag pcDNA3 or RelA cFlag pcDNA3 alone or along with either 1 µg of pEGFP-PARP7 or 0.8 µg of pEGFP-PARP7H532A using Lipofectamine™ 2000 (Invitrogen). After 24 h, cell lysis and co-immunoprecipitation was carried out as previously described [22 (link)]. The antibodies used for detection with Western blotting were anti-poly/mono-ADP-ribose (Cell Signaling Technology; E6F6A), anti-GFP (rabbit) (Abcam, Cambridge, United Kingdom; ab290), anti-GFP (mouse) (Clontech Laboratories, Mountain View, CA, USA; JL-8), anti-FLAG (rabbit) (Sigma Aldrich; F7425), and anti-FLAG (mouse) (Sigma-Aldrich; M2).

Rasmussen M., Alvik K., Kannen V., Olafsen N.E., Erlingsson L.A., Grimaldi G., Takaoka A., Grant D.M, & Matthews J. (2023). Loss of PARP7 Increases Type I Interferon Signaling in EO771 Breast Cancer Cells and Prevents Mammary Tumor Growth by Increasing Antitumor Immunity. Cancers, 15(14), 3689.

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Chikungunya virus nsP2 protein analysis

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The following reagents were used: β-NAD⁺ (Sigma), ³²P-NAD⁺ (Perkin-Elmer), IFNα (Peprotech), Olaparib (Selleck Chemicals), OUL35 (Tocris) [61 (link)], propidium iodide solution (Sigma), Protease inhibitor cocktail (Sigma), Glutathione-sepharose (Sigma), TALON metal affinity resin (BD Bioscience), GFP-Trap magnetic agarose beads (Chromotek, gtma), anti-GFP (Rockland, mouse monoclonal 600-301-215 M and goat polyclonal 600-101-215), anti-α-Tubulin (Sigma, T5168 and Santa Cruz, sc-23948), anti-MAR binding reagent (Millipore, MABE1076), anti-Poly/Mono-ADP Ribose (Cell Signaling, E6F6A), anti-nsP1 (obtained from Dr. Merits, see also [55 (link)]), anti-GST (clone 6G9), anti-PARP10 (clone 5H11 [17 (link)]), anti-PARP12 (Sigma, SAB2104087), anti-Actin (clone C4, BP Biomedicals), anti-HA (BioLegend, clone 16B12), goat-anti-rabbit-HRP (Jackson Immunoresearch, 111-035-144), goat-anti-mouse-HRP (Jackson Immunoresearch, 115-036-068), goat-anti-rat-HRP (Jackson Immunoresearch, 112-035-068), rabbit-anti-goat-HRP (Santa Cruz, sc-2768).
Rabbit polyclonal, purified CHIKV-nsP2-specific antibodies were generated by immunizing rabbits simultaneously with two peptides (aa570-584: CERKYPFTKGKWNINK, and aa740-755: CVLGRKFRSSRALKPP), both located in the C-terminal third of CHIKV nsP2 (performed by Eurogentec).

Krieg S., Pott F., Potthoff L., Verheirstraeten M., Bütepage M., Golzmann A., Lippok B., Goffinet C., Lüscher B, & Korn P. (2023). Mono-ADP-ribosylation by PARP10 inhibits Chikungunya virus nsP2 proteolytic activity and viral replication. Cellular and Molecular Life Sciences, 80(3), 72.

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