O-GlcNAc Antibody (HGAC85)


Western Blot: O-GlcNAc Antibody (HGAC85) [NB300-614] - Western blot analysis of O-GlcNAc expression in 1) HeLa, 2) NTERA-2, 3) PC-12 and 4) COS-7 cell lysates using untreated antibody on the left side and antibody ...read more
Immunohistochemistry-Paraffin: O-GlcNAc Antibody (HGAC85) [NB300-614] - IHC staining of O-GlcNAc in mouse colon using DAB with hematoxylin counterstain.

Product Details

Reactivity AllSpecies Glossary
Applications WB, ChIP, ELISA, ICC/IF, IHC, IHC-P, IP
This product is unpurified. The exact concentration of antibody is not quantifiable.

Order Details

O-GlcNAc Antibody (HGAC85) Summary

Heat-killed, pepsin-treated group A streptococci (Streptococcus pyogenes)
Recognizes beta-1,3 linked O-linked N-acetylglucosamine (O-GlcNAc) residues of streptococcal group A carbohydrate as well as O-GlcNAc glycosylated proteins
IgG3 Kappa
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Packaging, Storage & Formulations

Store at -20C. Avoid freeze-thaw cycles.
0.1% Sodium Azide
This product is unpurified. The exact concentration of antibody is not quantifiable.


Application Notes
This O-GlcNAc Antibody (HGAC85) is useful for Western blot, Chromatin Immunoprecipitation, ELISA, Immunocytochemistry/Immunofluorescence, Immunohistochemistry-Paraffin and Immunoprecipitation. ChIP assay reported in literature (PMID: 20368426). ICC and IP reported (Hamiel CR, et al). IHC reported (see Zhang X, et al). By Western blot, this antibody detects several proteins representing O-GlcNAc glycoproteins. Immunofluorescence staining of O-GlcNAc in cells results in labeling of the nuclear envelope and pores, nucleolus, and cytoplasm. This staining pattern is consistent with other methods of detecting O-GlcNAc moieties. DO NOT USE WITH DILUENTS CONAINING GLYCOSYLATED PROTEINS.
Read Publications using
NB300-614 in the following applications:

Reactivity Notes

All Species.


Specificity to O-GlcNAc was verified in Western blot (see Images) by incubation of NB300-614 with 50 mM N-acetylglucosamine (Sigma Cat. No. A3286).

Alternate Names for O-GlcNAc Antibody (HGAC85)

  • GlcNAc
  • O-linked N-acetylglucosamine


O-GlcNAc (O-linked N-acetylglucosamine) is one of the most abundant posttranslational modifications on nuclear and cytoplasmic proteins. Many cellular proteins, including nuclear pore, oncogene, cytoskeletal, heat shock, viral and transcription regulatory proteins contain single O-GlcNAc residues attached to serine or threonine residues. This modification occurs via the O-GlcNAc transferase (OGT). There appears to be a competitive modification at these residues. Either the residues are glycosylated or they are phosphorylated. Because of the significance of phosphorylation in cancer research, such competition can be of major interest. O-GlcNAc bearing proteins tend to be found in multimeric complexes. This has led to the suggestion that O-GlcNAc glycosylation may also obscure phosphorylation sites and acts as a signaling mechanism or mediator of signaling. Recent research has revealed that the O-GlcNAcylation of the EGF repeats of Notch are modified via a novel O-GlcNAc transferase, EOGT1 (PMID: 22310717).


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 O-GlcNAc Antibody (NB300-614)(9)

We have publications tested in 2 confirmed species: Rat, Primate.

We have publications tested in 2 applications: ICC/IF, WB.

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Showing Publications 1 - 9 of 9.
Publications using NB300-614 Applications Species
Yagi H, Nakagawa N, Saito T et al. AGO61-dependent GlcNAc modification primes the formation of functional glycans on alpha-dystroglycan. Sci Rep. 2013 Nov 21 [PMID:24256719] (WB, Primate) WB Primate
Love DC, Ghosh S, Mondoux MA et al. Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity. Proc Natl Acad Sci U S A. 2010 Apr. [PMID:20368426]
Hamiel CR, Pinto S, Hau A et al. Glutamine enhances heat shock protein 70 expression via increased hexosamine biosynthetic pathway activity. Am J Physiol Cell Physiol. 2009 Dec. [PMID:19776393]
Akimoto Y, Kreppel LK, Hirano H, Hart GW. Localization of the O-linked N-acetylglucosamine transferase in rat pancreas. Diabetes. 1999 Dec [PMID:10580430] (ICC/IF, Rat) ICC/IF Rat
Zhang X, Bennett V. Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier. J Biol Chem. 1996 Dec. [PMID:8940148]
Greenspan NS, Dacek DA, Cooper LJ. Fc region-dependence of IgG3 anti-streptococcal group A carbohydrate antibody functional affinity. I. The effect of temperature. J Immunol. 1988 Dec 15 [PMID:3058803]
Greenspan NS, Dacek DA, Cooper LJ. Cooperative binding of two antibodies to independent antigens by an Fc-dependent mechanism. FASEB J. 1989 Aug [PMID:2666233]
Greenspan NS, Monafo WJ, Davie JM. Interaction of IgG3 anti-streptococcal group A carbohydrate (GAC) antibody with streptococcal group A vaccine: enhancing and inhibiting effects of anti-GAC, anti-isotypic, and anti-idiotypic antibodies. J Immunol. 1987 Jan 1 [PMID:2431057]
Turner JR, Tartakoff AM, Greenspan NS. Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies. Proc Natl Acad Sci USA. 1990 Aug [PMID:2116002] (ICC/IF, Rat) ICC/IF Rat

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Product General Protocols

Video Protocols

WB Video Protocol
ChIP Video Protocol
ChIP Webinar
ICC/IF Video Protocol

FAQs for O-GlcNAc Antibody (NB300-614). (Showing 1 - 1 of 1 FAQs).

  1. Is it possible to get your mAb without BSA or sodium azide? I am interested in NB300-614 and NB300-524.
    • These antibodies are supplied in Sodium Azide, but if you are interested, we do provide kits to clean up the antibodies. Here is the link to our AbSelect Antibody Purification Kits.

Secondary Antibodies


Isotype Controls

Additional O-GlcNAc Antibody (HGAC85) Products

O-GlcNAc NB300-614

Research Areas for O-GlcNAc Antibody (NB300-614)

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Blogs on O-GlcNAc.

O-GlcNAc, Glucose Deprivation and Cancer
O-linked beta-N-acetylglucosamine (O-GlcNAc) is a sugar attachment to serine or threonine hydroxyl moieties on nuclear and cytoplasmic proteins. O-GlcNAc modified proteins are generally either cytoplasmic or nuclear proteins, and unlike asparagine-lin...  Read full blog post.

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