mouse monoclonal anti- o -glcnac (Avantor)

Avantor mouse monoclonal anti- o -glcnac

Mice fed an HCD or injected with thiamet G exhibit increased β-catenin and <t>O-GlcNAc</t> levels. A) Colon homogenates from mice fed an HCD or an SD for 9 wk were analyzed by Western blot for β-catenin, O-GlcNAc, and GAPDH (loading control) levels. OGTTs were performed, and blood glucose levels were determined for the HCD- and SD-fed mice by overnight food withdrawal after glucose force-feeding (differences are statistically nonsignificant). B) Colon homogenates from mice treated with the OGA inhibitor thiamet G for 2 wk were analyzed as in panel A. <t>Anti-O-GlcNAc</t> antibody condition was treated with free N-acetylglucosamine to show specificity. Glycemic levels were measured for the same animals with no significant differences observed. A, B) Average ± sd ratios of β-catenin/GAPDH and O-GlcNAc/GAPDH are shown. *P < 0.05, **P < 0.01, ***P < 0.001.

Mouse Monoclonal Anti O Glcnac, supplied by Avantor, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Mice fed an HCD or injected with thiamet G exhibit increased β-catenin and O-GlcNAc levels. A) Colon homogenates from mice fed an HCD or an SD for 9 wk were analyzed by Western blot for β-catenin, O-GlcNAc, and GAPDH (loading control) levels. OGTTs were performed, and blood glucose levels were determined for the HCD- and SD-fed mice by overnight food withdrawal after glucose force-feeding (differences are statistically nonsignificant). B) Colon homogenates from mice treated with the OGA inhibitor thiamet G for 2 wk were analyzed as in panel A. Anti-O-GlcNAc antibody condition was treated with free N-acetylglucosamine to show specificity. Glycemic levels were measured for the same animals with no significant differences observed. A, B) Average ± sd ratios of β-catenin/GAPDH and O-GlcNAc/GAPDH are shown. *P < 0.05, **P < 0.01, ***P < 0.001.

Journal: The FASEB Journal

Article Title: O -GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41

doi: 10.1096/fj.13-243535

Figure Lengend Snippet: Mice fed an HCD or injected with thiamet G exhibit increased β-catenin and O-GlcNAc levels. A) Colon homogenates from mice fed an HCD or an SD for 9 wk were analyzed by Western blot for β-catenin, O-GlcNAc, and GAPDH (loading control) levels. OGTTs were performed, and blood glucose levels were determined for the HCD- and SD-fed mice by overnight food withdrawal after glucose force-feeding (differences are statistically nonsignificant). B) Colon homogenates from mice treated with the OGA inhibitor thiamet G for 2 wk were analyzed as in panel A. Anti-O-GlcNAc antibody condition was treated with free N-acetylglucosamine to show specificity. Glycemic levels were measured for the same animals with no significant differences observed. A, B) Average ± sd ratios of β-catenin/GAPDH and O-GlcNAc/GAPDH are shown. *P < 0.05, **P < 0.01, ***P < 0.001.

Article Snippet: Mouse monoclonal anti- O -GlcNAc (RL2; VWR International, Fontenay-sous-Bois, France), mouse monoclonal anti-phosphoT41-β-catenin (C8616; Sigma-Aldrich), rabbit polyclonal anti-phospho-T41/S45-β-catenin (9565; Cell Signaling Technology, Leiden, The Netherlands), rabbit polyclonal anti-phospho-S33/S37/T41-β-catenin (9561; Cell Signaling Technology), and rabbit polyclonal anti-HA (Santa Cruz Biotechnology) were used at a final dilution of 1:1000.

Techniques: Injection, Western Blot

O-GlcNAcylation occurs in the D box of β-catenin and reduces its ubiquitinylation. A) MCF7 cells were cotransfected with vectors encoding FLAG-β-catenin and ubiquitin-HA and treated with siOGA and MG132. β-Catenin immunoprecipitates were analyzed by Western blot with anti-FLAG and anti-HA antibodies. B) Schematic representation of the β-catenin structure. The N-terminal region contains a D box, in which phosphorylation of 4 specific residues drives the ubiquitinylation and the subsequent proteasomal degradation of β-catenin. CK1α first phosphorylates S45, and then GSK3β successively modifies T41, S37, and S33. To investigate the O-GlcNAcylation of the D box, we used a mutant form of β-catenin in which these 4 phosphorylated residues were mutated into alanine (TM). The central region of β-catenin contains 12 imperfect sequence repeats of 42 aa (the armadillo repeats) that are essential in the interaction with many partners, including cadherins, APC, and TCF/LEF. The C-terminal region displays the transactivator function required for activation of target genes. C) MCF7 cells were transfected with FLAG-β-catenin (WT), TM-FLAG-β-catenin (TM), or an empty vector (Mock). At 48 h after transfection, the cells were lysed, and the lysates were analyzed by Western blot with anti-FLAG and -actin (loading control) antibodies. D) MCF7 cells were transfected with the vectors described above. At 36 h after transfection, the cells were treated with or without 5 mM glucosamine for 16 h and lysed, and β-catenin was immunoprecipitated with an anti-FLAG antibody. Immunoprecipitates were analyzed by Western blot with anti-O-GlcNAc and anti-FLAG antibodies. Average ± sd ratios of O-GlcNAcylated-β-catenin/total β-catenin are shown. **P < 0.01.

Journal: The FASEB Journal

Article Title: O -GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41

doi: 10.1096/fj.13-243535

Figure Lengend Snippet: O-GlcNAcylation occurs in the D box of β-catenin and reduces its ubiquitinylation. A) MCF7 cells were cotransfected with vectors encoding FLAG-β-catenin and ubiquitin-HA and treated with siOGA and MG132. β-Catenin immunoprecipitates were analyzed by Western blot with anti-FLAG and anti-HA antibodies. B) Schematic representation of the β-catenin structure. The N-terminal region contains a D box, in which phosphorylation of 4 specific residues drives the ubiquitinylation and the subsequent proteasomal degradation of β-catenin. CK1α first phosphorylates S45, and then GSK3β successively modifies T41, S37, and S33. To investigate the O-GlcNAcylation of the D box, we used a mutant form of β-catenin in which these 4 phosphorylated residues were mutated into alanine (TM). The central region of β-catenin contains 12 imperfect sequence repeats of 42 aa (the armadillo repeats) that are essential in the interaction with many partners, including cadherins, APC, and TCF/LEF. The C-terminal region displays the transactivator function required for activation of target genes. C) MCF7 cells were transfected with FLAG-β-catenin (WT), TM-FLAG-β-catenin (TM), or an empty vector (Mock). At 48 h after transfection, the cells were lysed, and the lysates were analyzed by Western blot with anti-FLAG and -actin (loading control) antibodies. D) MCF7 cells were transfected with the vectors described above. At 36 h after transfection, the cells were treated with or without 5 mM glucosamine for 16 h and lysed, and β-catenin was immunoprecipitated with an anti-FLAG antibody. Immunoprecipitates were analyzed by Western blot with anti-O-GlcNAc and anti-FLAG antibodies. Average ± sd ratios of O-GlcNAcylated-β-catenin/total β-catenin are shown. **P < 0.01.

Techniques: Western Blot, Mutagenesis, Sequencing, Activation Assay, Transfection, Plasmid Preparation, Immunoprecipitation

Perturbation of O-GlcNAc level disturbs the interaction between β-catenin and α-catenin. A) MCF7 cells were treated with the potent OGT inhibitor Ac5S-GlcNAc at a concentration of 100 μM for 16 h or with DMSO as a vehicle control and with MG132 at 1 μM. The cells were lysed, and coimmunoprecipitation was performed with an anti-β-catenin antibody. Nonimmune rabbit IgG was used as a negative control. Immunoprecipitates and 1% of whole-cell lysates (input) were analyzed by Western blot with the indicated antibodies. (Note that the anti-O-GlcNAc antibody was used with and without free N-acetylglucosamine.) B) MCF7 cells were transfected with a nontarget siRNA (siCtrl) or with an OGT siRNA (siOGT). The cells were treated with 1 μM MG132 for 16 h. At 72 h after transfection, the cells were lysed, and coimmunoprecipitation and Western blot analysis were performed as in panel A, C) The same procedure as in panel B was performed, except that an OGA siRNA (siOGA) was used.

Journal: The FASEB Journal

Article Title: O -GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41

doi: 10.1096/fj.13-243535

Figure Lengend Snippet: Perturbation of O-GlcNAc level disturbs the interaction between β-catenin and α-catenin. A) MCF7 cells were treated with the potent OGT inhibitor Ac5S-GlcNAc at a concentration of 100 μM for 16 h or with DMSO as a vehicle control and with MG132 at 1 μM. The cells were lysed, and coimmunoprecipitation was performed with an anti-β-catenin antibody. Nonimmune rabbit IgG was used as a negative control. Immunoprecipitates and 1% of whole-cell lysates (input) were analyzed by Western blot with the indicated antibodies. (Note that the anti-O-GlcNAc antibody was used with and without free N-acetylglucosamine.) B) MCF7 cells were transfected with a nontarget siRNA (siCtrl) or with an OGT siRNA (siOGT). The cells were treated with 1 μM MG132 for 16 h. At 72 h after transfection, the cells were lysed, and coimmunoprecipitation and Western blot analysis were performed as in panel A, C) The same procedure as in panel B was performed, except that an OGA siRNA (siOGA) was used.

Techniques: Concentration Assay, Negative Control, Western Blot, Transfection

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