O6014
Anti-O-GlcNAc Transferase (TI-14) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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Synonym(s):
Anti-O-linked N-Acetylglucosamine Transferase, Anti-OGT
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 110 kDa
species reactivity
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
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... OGT(8473)
mouse ... Ogt(108155)
rat ... Ogt(26295)
Related Categories
General description
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.
Immunogen
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)
Immunofluorescence (1 paper)
Biochem/physiol Actions
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.
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.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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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
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)
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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