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O6014

Sigma-Aldrich

Anti-O-GlcNAc Transferase (TI-14) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-O-linked N-Acetylglucosamine Transferase

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About This Item

Numéro MDL:
MFCD07370422
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 110 kDa

Espèces réactives

mouse, human, rat

Technique(s)

indirect immunofluorescence: 1:50-1:100 using A549 human lung carcinoma cells fixed with paraformaldehyde/triton
western blot: 1:1,000-1:2,000 using HeLa cell nuclear extracts

Numéro d'accès UniProt

O15294

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... OGT(8473)
mouse ... Ogt(108155)
rat ... Ogt(26295)

Description générale

O-GlcNAc transferase (OGT) catalyzes the addition of an N-acetylglucosamine residue to the amino acids serine or threonine. The enzyme is an homotrimer consisting of three subunits of 110 kDa each, with multiple tetratricopeptide (TPR) repeats.

Immunogène

synthetic peptide corresponding to amino acids 1024-1037 of human O-GlcNAc transferase, conjugated to KLH via an N-terminal added cysteine residue.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)

Actions biochimiques/physiologiques

O-linked β-N-acetyl glycosamine (O-GlcNAc) is involved in repressing transcription. O-GlcNAc transferase (OGT) interacts with a histone deacetylase complex by binding to the co repressor Sin3A. This interaction leads to the repression of transcription, after transcription factors and RNA polymerase II are modified by addition of O-GlcNAc. O-GlcNAc modification reversibly inhibits proteosomal function in an ubiquitin-independent fashion.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Sadia Raab et al.
Oncology letters, 23(4), 105-105 (2022-03-05)
Tumor occurrence and development are closely related to metabolism abnormalities. One of the metabolic networks that is dysregulated during carcinogenesis is the fatty acid synthesis pathway, which is mainly controlled by fatty acid synthase (FASN). We previously demonstrated in proliferating
Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
Comer FI and Hart GW
Biochemistry, 40(26), 7845-7852 (2001)
O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar
Wells L and Hart GW
Febs Letters, 546(1), 154-158 (2003)
Alexandre Berthier et al.
Proceedings of the National Academy of Sciences of the United States of America, 115(47), E11033-E11042 (2018-11-07)
The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions. An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein. By shielding cytoplasmic OGT from proteasomal degradation
Stéphanie Olivier-Van Stichelen et al.
Frontiers in genetics, 5, 256-256 (2014-08-20)
O-GlcNAc Transferase (OGT) catalyzes protein O-GlcNAcylation, an abundant and dynamic nuclear and cytosolic modification linked to epigenetic regulation of gene expression. The steady-state levels of O-GlcNAc are influenced by extracellular glucose concentrations suggesting that O-GlcNAcylation may serve as a metabolic
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