protein

Recombinant Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

MBS1123899

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

O-GlcNAc transferase subunit p110; O-linked N-acetylglucosamine transferase 110 kDa subunit; OGT

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit isoform 1; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; O-linked N-acetylglucosamine (GlcNAc) transferase; O-GlcNAc transferase subunit p110; O-linked N-acetylglucosamine transferase 110 kDa subunit; OGT

OGT

OGT; OGT; HRNT1; HINCUT-1; O-GLCNAC; OGT

OGT1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

606-1022

1046

MAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTK
GARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQET
SPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVID
FKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDG
GDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITIN
GFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPE
DAIVYCNFNQLYKIDPSTLQM

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Neuroscience

Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex. Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2

O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats.Lubas W.A., Frank D.W., Krause M., Hanover J.A.J. Biol. Chem. 272:9316-9324(1997) Human O-GlcNAc transferase (OGT) genomic structure, analysis of splice variants, fine mapping in Xq13.1.Nolte D., Muller U.Mamm. Genome 13:62-64(2002) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Bienvenut W.V., Dhillon A.S., Kolch W.Submitted (FEB-2008) to UniProtKB Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A coupling protein O-GlcNAcylation to transcriptional repression.Yang X., Zhang F., Kudlow J.E.Cell 110:69-80(2002) Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.Genes Dev. 17:896-911(2003) Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance.Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V., Kudlow J.E., Michell R.H., Olefsky J.M., Field S.J., Evans R.M.Nature 451:964-969(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease.Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K., Gong C.X.Brain 132:1820-1832(2009) Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux.Taylor R.P., Geisler T.S., Chambers J.H., McClain D.A.J. Biol. Chem. 284:3425-3432(2009) GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis.Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.Nature 459:455-459(2009) Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex.Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.J. Biol. Chem. 285:4268-4272(2010) Regulation of insulin receptor substrate 1 (IRS-1) /AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes.Whelan S.A., Dias W.B., Thiruneelakantapillai L., Lane M.D., Hart G.W.J. Biol. Chem. 285:5204-5211(2010) The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase a link between DYT6 and DYT3 dystonias.Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L., Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B., Kristie T.M., Girard J.P.J. Biol. Chem. 285:13364-13371(2010) Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis.Shin S.H., Love D.C., Hanover J.A.Amino Acids 40:885-893(2011) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G., Vogel J.L., Kristie T.M., Affar E.B.Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011) GlcNAcylation of histone H2B facilitates its monoubiquitination.Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S., Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F., Kitagawa H., Roeder R.G., Brown M., Kato S.Nature 480:557-560(2011) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) Phosphofructokinase 1 glycosylation regulates cell growth and metabolism.Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A. III, Peters E.C., Driggers E.M., Hsieh-Wilson L.C.Science 337:975-980(2012) TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS.Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., Murphy N., Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H., Levine R.L., Bernard O., Mercher T., Solary E., Urh M., Daniels D.L., Fuks F.EMBO J. 32:645-655(2013) TET2 promotes histone O-GlcNAcylation during gene transcription.Chen Q., Chen Y., Bian C., Fujiki R., Yu X.Nature 493:561-564(2013) O-GlcNAcylation regulates EZH2 protein stability and function.Chu C.S., Lo P.W., Yeh Y.H., Hsu P.H., Peng S.H., Teng Y.C., Kang M.L., Wong C.H., Juan L.J.Proc. Natl. Acad. Sci. U.S.A. 111:1355-1360(2014) The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha.Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A., Conti E.Nat. Struct. Mol. Biol. 11:1001-1007(2004) Structure of human O-GlcNAc transferase and its complex with a peptide substrate.Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S.Nature 469:564-567(2011)

32307148

NP_858058.1

NM_181672.2

O15294

62.5kD

Chromatin Modifying Enzymes Pathway (1270434); Chromatin Organization Pathway (1270433); HATs Acetylate Histones Pathway (1270435); Insulin Resistance Pathway (1272486); Other Types Of O-glycan Biosynthesis Pathway (82978); Other Types Of O-glycan Biosynthesis Pathway (349); Protein O-[N-acetyl]-glucosylation Pathway (1108787); Protein O-[N-acetyl]-glucosylation Pathway (982231)

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. [provided by RefSeq, Oct 2009]

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180