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OGT encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Additionally we are shipping OGT Proteins (5) and OGT Kits (4) and many more products for this protein.
Showing 10 out of 84 products:
Human Polyclonal OGT Primary Antibody for EIA, WB - ABIN453239
Fujiki, Chikanishi, Hashiba, Ito, Takada, Roeder, Kitagawa, Kato: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. in Nature 2009
Show all 3 references for ABIN453239
Human Polyclonal OGT Primary Antibody for IHC (p), WB - ABIN390649
Taylor, Geisler, Chambers, McClain: Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux. in The Journal of biological chemistry 2009
Show all 3 references for ABIN390649
Chicken Polyclonal OGT Primary Antibody for 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
Dog (Canine) Polyclonal OGT Primary Antibody for WB - ABIN374838
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
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.
We concluded that OGT plays a key role in gastric cancer proliferation and survival, and could be a potential target for therapy.
Data suggest RNA polymerase II (POLR2A (show POLR2A Antibodies)) is extensively modified on its unique C-terminal domain (CTD) by O-GlcNAc transferase (OGT); efficient O-GlcNAcylation requires a minimum of 20 heptad CTD repeats in POLR2A (show POLR2A Antibodies) and more than half of NTD of OGT.
Together, these findings suggest that induction of SNO (show SKIL Antibodies)-OGT by Ab exposure is a pathogenic mechanism to cause cellular hypo-O-GlcNAcylation by which Ab neurotoxicity is executed
These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression.
These results demonstrate that distinct OGT-binding sites in HCF-1 (show HCFC1 Antibodies) promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
This work reveals that although the N-terminal TPR repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site specificity.
OGT expression is increased under hypoxic conditions.
E2F1 (show E2F1 Antibodies) negatively regulates both Ogt and Mgea5 (show MGEA5 Antibodies) expression in an Rb1 (show RB1 Antibodies) protein-dependent manner.
Inhibition of O-Linked N-Acetylglucosamine Transferase Reduces Replication of Herpes Simplex Virus and Human Cytomegalovirus.
miR4235p was associated with congestive heart failure and the expression levels of proBNP; in addition, OGT was found to be a direct target of miR4235p.
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)).
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
The hyperphagia derived from the paraventricular nucleus of the hypothalamus, where loss of OGT was associated with impaired satiety.
26S proteasome (show Psmd4 Antibodies)-mediated OGT reduction contributed to hypoxia-induced vascular endothelial inflammatory response.
Glucosamine-induced OGT activation mediates glucose production through cleaved Notch1 (show NOTCH1 Antibodies) and FoxO1 (show FOXO1 Antibodies), which contributes to the regulation of maintenance of self-renewal in mouse embryonic stem cells.
Study shows that OGT expression is enriched in hypothalamic AgRP (show AGRP Antibodies) neurons and induced by fasting and ghrelin (show GHRL Antibodies). Pharmacogenetical activation of AgRP (show AGRP Antibodies) neurons suppresses the thermogenic program in white fat (WAT), while the selective knockout of Ogt in AgRP (show AGRP Antibodies) neurons inhibits neuronal activity, promotes WAT browning, and protects mice against diet-induced obesity.
OGT serves as a key placental biomarker and functions as an important mediator of the maternal changes occurring in response to stress.
cardiomyocyte-specific OGT KO mice had dilated hearts, signs of heart failure and low viability.
Treatment with GlcN, in contrast, inhibits LPS (show TLR4 Antibodies)-ind inflammation and decreased LPS (show TLR4 Antibodies)-mediated recruitment of OGT, mSin3A, and HDACs.
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