Anti o glcnac

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-O-GlcNAc is a laboratory reagent used to detect and quantify O-linked N-acetylglucosamine (O-GlcNAc) modifications on proteins. O-GlcNAc is a post-translational modification that plays a crucial role in various cellular processes. Anti-O-GlcNAc provides a tool to study the dynamics and functions of this important modification.

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Lab products found in correlation

Anti ogt, by Merck Group (3 mentions) Anti actin, by Santa Cruz Biotechnology (2 mentions) Image studio software, by LI COR (2 mentions) Irdye 680 or 800 conjugated secondary antibodies, by LI COR (2 mentions) Hrp conjugated anti mouse igm antibody, by LI COR (2 mentions) Anti β actin, by Abcam (2 mentions) Odyssey fc imaging system, by LI COR (2 mentions) Anti oga, by Merck Group (2 mentions) Anti β actin, by Merck Group (1 mentions) Anti flag, by Merck Group (1 mentions) Anti p65, by Santa Cruz Biotechnology (1 mentions) Anti iκbα, by Cell Signaling Technology (1 mentions) Anti nanog, by Cell Signaling Technology (1 mentions) Anti cd44, by Cell Signaling Technology (1 mentions) Anti ogt, by Santa Cruz Biotechnology (1 mentions) Anti c myc, by Novus Biologicals (1 mentions) Anti klf8, by Merck Group (1 mentions) Anti k14, by Thermo Fisher Scientific (1 mentions) Anti vimentin, by Cell Signaling Technology (1 mentions) Anti fibronectin, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

O-GlcNAc (5 citations) Mouse anti-O-GlcNAc transferase (C-10) (2 citations)

6 protocols using anti o glcnac

Quantification of NF-κB Pathway Proteins

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Cells were cultured to about 90–95% confluence before lysis. Whole cell samples were collected and lysed using Radio Immunoprecipitation Assay buffer (RIPA buffer: 150 mM NaCl, 0.1% Triton X-100, 0.5% sodium deoxycholate, 0.1% sodium dodecyl sulfate (SDS), 50 mM Tris-HCl pH 8.0, and protease inhibitors). Whole cell lysates were separated by SDS/PAGE gels, and proteins were probed by Western blotting. Antibodies used to detect the target proteins include anti-p65 (Santa Cruz Biotechnology, sc-372, Dallas, TX, USA), anti-FLAG (Sigma-Aldrich, F1804, St. Louis, MI, USA), anti-O-GlcNAc (Santa Cruz Biotechnology, sc-59623, Dallas, TX, USA), anti-IκBα (Cell signaling technology, 9242s, Dallas, TX, USA), anti-pS536 (Cell signaling, ab3031, Danvers, MA, USA), and anti-beta actin (Sigma-Aldrich, A5316, St. Louis, MO, USA). Quantifica-tions were performed using ImageJ on three inde-pendent western blot images.

Motolani A., Martin M., Wang B., Jiang G., Alipourgivi F., Huang X., Safa A., Liu Y, & Lu T. (2023). Critical Role of Novel O-GlcNAcylation of S550 and S551 on the p65 Subunit of NF-κB in Pancreatic Cancer. Cancers, 15(19), 4742.

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Western Blotting of Mammosphere Proteins

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Western blotting procedures were carried out as previously described (15 ). Briefly, cells were collected in RIPA lysis buffer (150mM NaCl, 1% NP40, 0.5% DOC, 50mM Tris-HCl at pH 8, 0.1% SDS, 10% glycerol, 5mM EDTA, 20mM NaF and 1mM Na₃VO₄, 1 μg/ml each of pepstatin, leupeptin, and aprotinin, 200 μg/ml phenyl-methylsulfonyl-fluoride). Lysates were cleared by centrifugation at 14,000 x g for 20 minutes at 4 °C and analyzed by SDS-PAGE and autoradiography. Lysates from mammospheres were collected 7 days after culture in mammosphere media. Corresponding adherent controls were put on mammosphere media 24 hrs after seeding and collected the next day. Antibodies were purchased from the following companies; Anti-OGT (Santa Cruz, Cell-Signaling), Anti-O-GlcNAc (Santa Cruz, Sigma), Anti-c-Myc (Novus), Anti-Actin (Santa Cruz), Anti-CD44, Anti-Fibronectin, Anti-Vimentin, Anti-NANOG (Cell-Signaling), Anti-K8/18 (Thermo-Fisher), Anti-K14 (Thermo-Fisher), Anti-GAPDH (Genscript), Anti-KLF8 (Sigma). Densitometry was performed using Image J Software (National Institutes of Health, Bethesda, MA).

Akella N.M., Le Minh G., Ciraku L., Mukherjee A., Bacigalupa Z.A., Mukhopadhyay D., Sodi V.L, & Reginato M.J. (2020). O-GlcNAc Transferase Regulates Cancer Stem-like Potential of Breast Cancer Cells. Molecular cancer research : MCR, 18(4), 585-598.

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Protein Extraction and Western Blot Analysis

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Cells were collected in RIPA lysis buffer (150mM NaCl, 1% NP40, 0.5% DOC, 50mM Tris-HCl at pH 8, 0.1% SDS, 10% glycerol, 5mM EDTA, 20mM NaF and 1mM Na₃VO₄, 1 μg/ml each of pepstatin, leupeptin, and aprotinin, 200 μg/ml phenyl-methylsulfonyl-fluoride). Lysates were cleared by centrifugation at 14,000 x g for 20 minutes at 4 °C and analyzed by SDS-PAGE and autoradiography. Western blots were then analyzed with the following antibodies; anti-Actin, anti-c-MYC, anti-ERK2 (D-2), anti-O-GlcNAc (RL2), anti-Cyclin D1 (Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-phospho-Akt (Ser473), anti-phospho-Akt (T308), anti- P70 S6 Kinase, anti-Tuberin/TSC2, anti-AKT, anti-phospho-P70-S6 Kinase (T389) and anti-phospho-4EBP1 (T70), anti-4EBP1 (53H17), Cleaved Caspase 3 (D175), anti-BIM, anti-CHOP (L63F7), anti-phospho-eIF2α, anti-eIF2α (Cell Signaling, Danvers, MA, USA), anti-phospho-ERK (T185/Y187) (Invitrogen Corporation, Carlsbad, CA, USA), anti-OGT, anti-O-GlcNAc (CTD110.6) (Sigma, St Louis, MO, USA), anti-HSP90 alpha (Enzo Life Sciences, Farmingdale, NY, USA) and anti-MGEA5 (OGA) (Proteintech Group, Chicago, IL, USA). Densitometry was performed using Image J Software (National Institutes of Health, Bethesda, MA).

Sodi V.L., Khaku S., Krutilina R., Schwab L.P., Vocadlo D.J., Seagroves T.N, & Reginato M.J. (2015). mTOR/MYC Axis Regulates O-GlcNAc Transferase (OGT) Expression and O-GlcNAcylation in Breast Cancer. Molecular cancer research : MCR, 13(5), 923-933.

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Standardized Molecular Analyses of OGT and OGA

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Standard molecular procedures for RNA analyses, western blotting, and plasmid construction are described in the Supplemental Experimental Procedures. Oligonucleotides are listed in Table S1. Antibodies used were: anti-OGT (Sigma, O6264), anti-OGA (Sigma, SAB4200267), anti-O-GlcNAc (CTD110.6; Santa Cruz Biotechnologies, SC-59623 or RL-2; Thermo Fisher Scientific, MA1-072), and/or anti-β-actin (Abcam, ab6276). IRDye-680 or -800 conjugated secondary antibodies (LI-COR Bioscience) and HRP conjugated anti mouse IgM antibody (CTD110.6 only) were used to visualize the detected protein bands through an Odyssey Fc Imaging System and quantitative analyses were performed using ImageStudio software (LI-COR Bioscience).

Park S.K., Zhou X., Pendleton K.E., Hunter O.V., Kohler J.J., O'Donnell K.A, & Conrad N.K. (2017). A Conserved Splicing Silencer Dynamically Regulates O-GlcNAc Transferase Intron Retention and O-GlcNAc Homeostasis. Cell reports, 20(5), 1088-1099.

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Western Blot Analysis of Protein Expression

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Proteins (40 µg) were separated on a 7.5% stain-free SDS-polyacrylamide gel by electrophoresis then transferred to mini low fluorescence PVDF membranes (Bio-Rad Laboratories, Hemel Hempstead, UK) and visualised using the Chemidoc MP imaging system (Bio-Rad Laboratories). The membrane was blocked with 3.5% (w/v) TBS-Tween (10 mmol/L Tris pH 8, 150 mmol/L NaCl, 0.1% Tween 2.0) for 1 h at room temperature (RT). Appropriate primary antibody was added and incubated overnight at 4°C (anti-eNOS 1:200, anti-peNOS^ser1177 1:200, anti-O-GlcNAc 1:200; Santa Cruz Biotechnology, Dallas, TX, USA; anti-AMPKα 1:1,000 and anti-pAMPKα 1:1,000; Cell Signalling, Hitchin, UK) followed by exposure to a horseradish peroxidase-conjugated secondary antibody for 1 h at RT. Chemiluminescence was performed with Clarity Western ECL Substrate (Bio-Rad Laboratories) and images were obtained using the Chemidoc MP imaging system. Immunoblots were analysed using ImageLab 5.2.1 (Bio-Rad Laboratories) software and adjusted to the total protein of the sample as previously described [35 (link)].

Zaborska K.E., Edwards G., Austin C, & Wareing M. (2017). The Role of O-GlcNAcylation in Perivascular Adipose Tissue Dysfunction of Offspring of High-Fat Diet-Fed Rats. Journal of Vascular Research, 54(2), 79-91.

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Standardized Molecular Analyses of OGT and OGA

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