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anti-Rat (Rattus) OGT Antibodies:
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All Species Monoclonal OGT Primary Antibody for ChIP, ICC - ABIN152767
Akimoto, Kreppel, Hirano, Hart: Localization of the O-linked N-acetylglucosamine transferase in rat pancreas. in Diabetes 1999
Show all 9 Pubmed References
Cow (Bovine) Monoclonal OGT Primary Antibody for ChIP, DB - ABIN152683
Dias, Cheung, Hart: O-GlcNAcylation of kinases. in Biochemical and biophysical research communications 2012
Show all 5 Pubmed References
Chemical Monoclonal OGT Primary Antibody for IP, WB - ABIN2668989
Comer, Vosseller, Wells, Accavitti, Hart: Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. in Analytical biochemistry 2001
Show all 2 Pubmed References
Mouse (Murine) Polyclonal OGT Primary Antibody for ELISA, WB - ABIN252910
Majumdar, Wright, Markowitz, Martinez-Hernandez, Raghow, Solomon: Insulin stimulates and diabetes inhibits O-linked N-acetylglucosamine transferase and O-glycosylation of Sp1. in Diabetes 2004
Human Polyclonal OGT Primary Antibody for ICC, IF - ABIN442747
Ise, Goto, Komura, Akaike: Engulfment and clearance of apoptotic cells based on a GlcNAc-binding lectin-like property of surface vimentin. in Glycobiology 2012
Cow (Bovine) Polyclonal OGT Primary Antibody for IHC, WB - ABIN2783662
Taylor, Parker, Hazel, Soesanto, Fuller, Yazzie, McClain: Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase. in The Journal of biological chemistry 2008
Cow (Bovine) Monoclonal OGT Primary Antibody for ELISA, FACS - ABIN4341246
Swamy, Pathak, Grzes, Damerow, Sinclair, van Aalten, Cantrell: Glucose and glutamine fuel protein O-GlcNAcylation to control T cell self-renewal and malignancy. in Nature immunology 2016
Here is presented a novel O-GlcNAc transferase (OGT), EOGT (show C3orf64 Antibodies), responsible for extracellular O-linked-N-acetylglucosamine acylation.
study found that the super sex combs (sxc)gene encodes O-linked N-acetylglucosamine transferase (Ogt); Polycomb (show CBX2 Antibodies) repression appears to be a critical function of Sxc/Ogt in Drosophila and may be mediated by the glycosylation of Polyhomeotic
Developmental regulation of zOGT transcriptional variants generated by alternative splicing and characterization of their OGT activities of protein O-GlcNAcylation.
Overexpression of Ogt delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer.
Hsp90 is involved in the regulation of OGT and O-GlcNAc modification and that Hsp90 inhibitors might be used to modulate O-GlcNAc modification and reverse its adverse effects in human diseases.
Findings indicate O-linked N-acetylglucosamine transferase (OGT) as a cellular factor involved in human papillomaviruses type 16/18 E6 and E7 expressions and cervical cancer tumorigenesis, suggesting that targeting OGT in cervical cancer may have potential therapeutic benefit.
The findings suggest that OGT promotes the O-GlcNAc modification of HDAC1 (show HDAC1 Antibodies) in the development of progression hepatocellular carcinoma.
Tax (show CNTN2 Antibodies) interacts with the host OGT/OGA (show MGEA5 Antibodies) complex and inhibits the activity of OGT-bound OGA (show MGEA5 Antibodies).
We identified two human PRC2 complexes and two PR-DUB deubiquitination complexes, which contain the O-linked N-acetylglucosamine transferase OGT1 and several transcription factors.
Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability
This work uncovers that URI (show C19orf2 Antibodies)-regulated OGT confers c-MYC (show MYC Antibodies)-dependent survival functions in response to glucose fluctuations.
The results of this study showed that the OGT is essential for sensory neuron survival and target innervation.
The authors show that O-GlcNAcylation of KEAP1 (show KEAP1 Antibodies) by OGT at serine 104 is required for the efficient ubiquitination and degradation of NRF2 (show GABPA Antibodies).
Data suggest that O-GlcNAc transferase 1 (OGT1) specifically binds to, O-GlcNAcylates, and stabilizes nonspecific lethal protein3 (NSL3 (show KANSL3 Antibodies)); stabilization of NSL3 (show KANSL3 Antibodies) by OGT1 up-regulates global acetylation levels of histone 4 at Lys-5 (show AASDHPPT Antibodies), Lys (show LYZ Antibodies)-8, and Lys (show LYZ Antibodies)-16.
conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 (show FOXA1 Antibodies) stability. These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
Data suggest that enzymes in hexosamine biosynthesis pathway and downstream protein O-GlcNAcylation are important for preimplantation development (show MTA2 Antibodies); these include Ogt, Gfpt (glutamine (show GFPT1 Antibodies)-fructose-6-P aminotransferase), and Oga (O-GlcNAcase (show MGEA5 Antibodies)).
O-GlcNAc modification is essential for cold-induced thermogenesis and mitochondrial biogenesis in brown adipose tissue.
This study identifies OGT activity as an important regulator of SC functions such as myelin maintenance and axonal support.
cullin 3 (CUL3 (show CUL3 Antibodies)), a cullin family E3 ubiquitin ligase (show MUL1 Antibodies), down-regulates the expression of the O-GlcNAc transferase (OGT) and inhibits STAT3 (show STAT3 Antibodies) O-GlcNAcylation.
OGT functions in metastatic spread of HPV E6/E7-positive tumor cells to the lungs through E6/E7, HCF-1 (show HCFC1 Antibodies) and CXCR4 (show CXCR4 Antibodies)
Furthermore, both Ogt and Oga (show MGEA5 Antibodies) were required for the reversion from primed ESD (show ESD Antibodies)-EpiSCs to naive rESCs. These findings indicate that O-GlcNAcylation plays an important role in the survival of primed ESD (show ESD Antibodies)-EpiSCs and in their reversion to naive rESCs.
Beyond its well-known role in adding beta-O-GlcNAc to serine and threonine residues of nuclear and cytoplasmic proteins, OGT also acts as a protease in the maturation of the cell cycle regulator (show CDKN2A Antibodies), HCF-1 (show HCFC1 Antibodies), and serves as an integral member of several protein complexes, many of them linked to gene expression. (Review)
the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNAc-transferase (OGT) and O-GlcNAcase (OGA (show MGEA5 Antibodies)), interact with the (A)gamma-globin (show HBG1 Antibodies) promoter at the -566 GATA repressor (show ZBTB32 Antibodies) site
OGT overexpression increased the level of OGA (show MGEA5 Antibodies), suggesting a compensatory mechanism for the aberrant O-GlcNAcylation.
O-GlcNAc transferase is at least partially required for maintaining cellular proliferative and migratory capacities of cardiomyocytes
This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains multiple tetratricopeptide repeats that are required for optimal recognition of substrates. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)
, O-linked GlcNAc transferase
, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase
, O-linked N-acetylglucosamine transferase
, lethal (2) NC130
, O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase) 1
, copy I
, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
, o-linked GlcNAc transferase
, TPR repeat-containing protein
, UDP-N-acetylglucosamine:peptide N-acetylglucosaminyltransferase
, O linked N-acetylglucosamine transferase
, O-GlcNAc transferase subunit p110
, O-linked N-acetylglucosamine transferase 110 kDa subunit
, UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase
, O-GlcNAc transferase p110 subunit
, uridinediphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyl transferase
, O linked N-acetylglucosamine transferase like