Date published: 2025-10-16

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O-GlcNAc Antibody (CTD110.6): sc-59623

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Datasheets
  • O-GlcNAc Antibody (CTD110.6) is a mouse monoclonal IgM κ O-GlcNAc antibody, cited in 71 publications, provided at 200 µg/ml
  • raised against O-GlcNAc containing serine-O-linked N-acetylglucosamine
  • recommended for detection of Ser-O-GlcNAc and Thr-O-GlcNAc of a broad range of species, including mammals, insects, worms, plants and filamentous fungi origin by WB and IP; non cross-reactive with peptide determinants or other closely-related carbohydrate antigens
  • See O-GlcNAc (RL2): sc-59624 for O-GlcNAc antibody conjugates, including AC, HRP, FITC, PE, Alexa Fluor® 488, 594, 647, 680 and 790.
  • At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for O-GlcNAc Antibody (CTD110.6). This work is in progress.

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O-GlcNAc Antibody (CTD110.6) is a mouse monoclonal IgM antibody that detects O-GlcNAc protein across mammals, insects, worms, plants, and filamentous fungi through western blotting (WB) and immunoprecipitation (IP). O-GlcNAc Antibody (CTD110.6) is available as a non-conjugated anti-O-GlcNAc antibody (CTD110.6). O-GlcNAc (O-linked N-acetylglucosamine) represents a unique protein glycosylation form occurring exclusively in eukaryotic cell nuclei and cytoplasm, playing a critical role in various cellular processes. This modification occurs on serine and threonine residues, influencing protein function and interactions. Heavily O-GlcNAcylated proteins often regulate nuclear transport, essential for maintaining cellular homeostasis and stress response. Dynamic interplay between O-GlcNAcylation and phosphorylation creates reversible multimeric complexes, enabling fine-tuned regulation of protein activity and signaling pathways. O-GlcNAcylation involvement in cancer and neurodegenerative disorders highlights significant implications in health and disease. Anti-O-GlcNAc antibody (CTD110.6) enables researchers to explore O-GlcNAc′s role in cellular functions and potential therapeutic applications.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.

Alexa Fluor® is a trademark of Molecular Probes Inc., OR., USA

LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences

O-GlcNAc Antibody (CTD110.6) References:

  1. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny.  |  Shafi, R., et al. 2000. Proc Natl Acad Sci U S A. 97: 5735-9. PMID: 10801981
  2. Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex.  |  Akimoto, Y., et al. 2003. Brain Res. 966: 194-205. PMID: 12618343
  3. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.  |  Haltiwanger, RS., et al. 1992. J Biol Chem. 267: 9005-13. PMID: 1533623
  4. Identification of secret agent as the O-GlcNAc transferase that participates in Plum pox virus infection.  |  Chen, D., et al. 2005. J Virol. 79: 9381-7. PMID: 16014901
  5. A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates.  |  Leavy, TM. and Bertozzi, CR. 2007. Bioorg Med Chem Lett. 17: 3851-4. PMID: 17531489
  6. Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance.  |  Yang, X., et al. 2008. Nature. 451: 964-9. PMID: 18288188
  7. O-GlcNAc Transferase: Structural Characteristics, Catalytic Mechanism and Small-Molecule Inhibitors.  |  Ju Kim, E. 2020. Chembiochem. 21: 3026-3035. PMID: 32406185
  8. Advances in chemical probing of protein O-GlcNAc glycosylation: structural role and molecular mechanisms.  |  Saha, A., et al. 2021. Chem Soc Rev. 50: 10451-10485. PMID: 34338261
  9. Integration of O-GlcNAc into Stress Response Pathways.  |  Fahie, KMM., et al. 2022. Cells. 11: PMID: 36359905
  10. O-GlcNAc modification of GSDMD attenuates LPS-induced endothelial cells pyroptosis.  |  Yu, F., et al. 2024. Inflamm Res. 73: 5-17. PMID: 37962578
  11. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats.  |  Kreppel, LK., et al. 1997. J Biol Chem. 272: 9308-15. PMID: 9083067
  12. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats.  |  Lubas, WA., et al. 1997. J Biol Chem. 272: 9316-24. PMID: 9083068

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

O-GlcNAc Antibody (CTD110.6)

sc-59623
200 µg/ml
$316.00

I need specifically detect O-GlcNAcylation un plant proteim extractos. We found lack of specificity using CTD110.6. Employment of a secondary anti-IgM is mandatory? It could be conveniente to use RL2?

Asked by: Salamandra
Thank you for your question. It would be helpful if you could call us, allowing for a more interactive discussion of this and other related questions.
Answered by: Technical Support
Date published: 2021-07-23

I am planning to IP this modification after protein digestion to peptides and wonder if the antibody recognise digested peptides carrying this modifications and if you would expect some specificity for certain peptides?

Asked by: Paolo
Thank you for your question. Unfortunately I do not have any information regarding if this antibody can detect digested peptides.
Answered by: Tech Service
Date published: 2019-04-09

What is the best way to avoid background when working on mouse samples with this mouse monoclonal antibody?

Asked by: AbPolly
Thank you for your inquiry. Our new line of Mouse IgG binding proteins can help reduce non-specific staining with mouse samples. A complete list of available binding proteins is available on our website here: https://www.scbt.com/scbt/browse/support-products-mouse-igg-binding-proteins/_/N-ecrety You can also use our alternative O-GlcNAc antibody sc-59624 in a variety of direct conjugations to reduce non-specific staining with mouse samples.
Answered by: Technical Service
Date published: 2016-12-22
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Rated 5 out of 5 by from goodvery nice,it work well in WB。Good specificity,nonspecific bands
Date published: 2021-07-31
Rated 4 out of 5 by from clear signal in immunofluorescence, dirty in WBThis antibody worked well in immunofluorescence in cell culture and also in paraffin embedded human brain tissue. In western blot, it needs a lot of washes after primary antibody especially, usually the first time there's a dark smear everywhere and if exposure is less than 5 min there's no signal. Usually after re-application of the secondary the signal gets clearer, perhaps due to longer washing of primary. Primary seems to stick, but this is a problem of this clone, not of this product in particular. Here are the captions again for the vertical (tissue) and horizontal (cells) IF pictures and the western blot since they did not fit in the space given: Cells: Immunofluorescence for O-GlcNAc in human astrocytes. A) no primary antibody. B) DMSO treatment (control). C) 200 uM Voc OGT inhibitor treatment. D) 100 uM 9D OGA inhibitor treatment. Green: O-GlcNAc (Santa Cruz CTD110.6), Blue: DAPI. Primary antibody was used at 1:100 dilution overnight in 5% goat serum in PBS. Secondary antibody was Goat anti-mouse IgM Alexafluor 488 conjugate. Tissue: Immunofluorescence in human tissue. A) IF of formalin fixed paraffin embedded human brain tissue. Control patient in his 60s. B) Alzheimer’s disease patient in his 60s. Green: O-GlcNAc. Blue: DAPI. Tissues were reparaffinized, rehydrated, antigen retrieval was performed in boiling citrate buffer, free formaldehydes were blocked with sodium borohydride. Blocking and antibody incubations were done in 5% goat serum in PBS. Lipofuscin was blocked with Sudan black for 20 min. after DAPI incubation. Western blot: Western blot with human astrocyte lysates. Multiple samples were run on SDS-PAGE gels and transferred to PVDF membrane. Blocking was with 5% milk in TBST. Primary antibody was used at 1:100 dilution in 5% BSA in TBST. Secondary antibody (rabbit anti-mouse IgM HRP) was diluted 1:1000 in 5% milk in TBST. Membrane was washed 2x 5 mins then 30 min in TBST after primary and then 3x 5 min after secondary. Imaging was for 10 mins.
Date published: 2020-12-30
Rated 5 out of 5 by from good result do WBWe used this antibody recenlty and following the struction choose the dilution 1:400(we feel it can diluted more),the band is right size,very good result.
Date published: 2018-05-26
Rated 4 out of 5 by from Worked wellI bought antibody for pilot experiments and it woked well in Western. I will be happy to buy more for future work.
Date published: 2018-02-16
Rated 5 out of 5 by from Really good !I used this antibody several times. It works well on human lung cells. even using a low dilution
Date published: 2017-07-05
Rated 5 out of 5 by from Great for Western blotMonoclonal O-GlcNAc (CTD110.6) antibody has been validated by Western blot. Highly recommended!
Date published: 2016-12-19
Rated 5 out of 5 by from Publishable WBPublishable WB.CoIP data with rat aortic smooth muscle cells - SCBT Publication Review
Date published: 2015-04-10
Rated 4 out of 5 by from Dirty blot but produced bands at expectedDirty blot but produced bands at expected MW in HeLa nuclear extract and A549 whole cell lysate and mouse brain tissue extract. -SCBT QC
Date published: 2015-03-26
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O-GlcNAc Antibody (CTD110.6) is rated 4.7 out of 5 by 10.
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