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Merck
CN

05-1245

Anti-O-GlcNAc Antibody, clone 9D1.E4(10)

clone 9D1.E4(10), from mouse

Synonym(s):

O-GlcNAc transferase p110 subunit, O-GlcNAc transferase subunit p110, O-linked GlcNAc transferase, O-linked N-acetylglucosamine (GlcNAc) transferase

(UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase, O-linked N-acetylglucosam

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Key Documents

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biological source

mouse

Quality Level

100

antibody form

purified antibody

antibody product type

primary antibodies

clone

9D1.E4(10), monoclonal

species reactivity

human

technique(s)

western blot: suitable

isotype

IgG1

NCBI accession no.

NP_858058.1

UniProt accession no.

O15294

shipped in

wet ice

target post-translational modification

glycosylation

Gene Information

human ... OGT(8473)

General description

O-linked N-acetylglucosamine (O-GlcNAc), is a member of the O-GlcNAc transferase family. O-GlcNAc is a posttranslational modification characterized by the attachment of N-acetylglucosamine to specific serine/threonine hydroxyl groups. It plays an important role in nutrient sensing, gene expression, and protein degradation. O-GlcNAc is widely expressed in the pancreas and is present in smaller amounts in skeletal muscle, heart, brain and placenta.
Various

Immunogen

SANM-conjugated linear peptide corresponding to human O-GlcNAc.

Application

Detect O-GlcNAc using this Anti-O-GlcNAc Antibody, clone 9D1.E4(10) validated for use in WB.
Research Category
Signaling
Research Sub Category
General Post-translation Modification

Biochem/physiol Actions

This antibody recognizes O-GlcNAc.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal antibody in 0.1M Tris-Glycine (pH7.4) 150mM NaCl with 0.05% sodium azide.

Preparation Note

Maintain refrigerated at 2-8°C for up to 12 months.

Analysis Note

Control
HEK293 cell lysate
Evaluated by Western Blot in O-GlcNAc transferease transfected HEK293 cell lysate and O-GlcNAcase transfected transfected HEK293 cell lysate.
Western Blot Analysis: 0.5 µg/mL of this antibody detected O-GlcNAc on 10 µg of
O-GlcNAc transferease transfected HEK293 cell lysate and O-GlcNAcase transfected transfected HEK293 cell lysate.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Chang Li et al.
Scientific reports, 11(1), 11272-11272 (2021-05-30)
O-GlcNAcylation, an energy-sensitive posttranslational modification, can regulate the activity of endothelial nitric oxide synthase (eNOS). Previous studies found that Thr866 is the key site for low-glucose-mediated regulation of eNOS O-GlcNAc. However, it is not known whether this activity functions through
Alazne Arrazola Sastre et al.
Cells, 12(14) (2023-07-29)
Protein O-GlcNAcylation has been associated with neurodegenerative diseases such as Alzheimer's disease (AD). The O-GlcNAcylation of the Amyloid Precursor Protein (APP) regulates both the trafficking and the processing of the APP through the amyloidogenic pathway, resulting in the release and
Luyun Zou et al.
The Journal of biological chemistry, 287(41), 34419-34431 (2012-08-22)
The posttranslational modification of nuclear and cytosolic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) has been shown to play an important role in cellular response to stress. Although increases in O-GlcNAc levels have typically been thought to be substrate-driven, studies in several
Characterization of the specificity of O-GlcNAc reactive antibodies under conditions of starvation and stress.
Reeves, RA; Lee, A; Henry, R; Zachara, NE
Analytical biochemistry null
Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc.
Teo, Chin Fen, et al.
Nature chemical biology, 6, 338-343 (2010)
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