O-Linked N-Acetylglucosamine (GlcNAc) Transferase (UDP-N-Acetylglucosamine:polypeptide-N-Acetylglucosaminyl Transferase) (OGT) (C-Term) Peptide

Details for Product No. ABIN696121, Supplier: Log in to see
Protein Name
  • BcDNA:GH04245
  • CG10392
  • Dmel\\CG10392
  • OGT
  • Ogt
  • P1201
  • SXC
  • Sxc
  • l(2)02637
  • l(2)NC130
  • sxc/Ogt
  • fm81g08
  • ogt
  • wu:fc12b01
  • wu:fm81g08
  • HRNT1
  • 1110038P24Rik
  • 4831420N21Rik
  • AI115525
  • Ogtl
  • O-linked N-acetylglucosamine (GlcNAc) transferase
  • super sex combs
  • O-linked N-acetylglucosamine (GlcNAc) transferase, tandem duplicate 1
  • O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)
  • O-linked GlcNAc transferase
  • o-linked GlcNAc transferase
  • ogt
  • sxc
  • ogt.1
  • OGT
  • GL50803_12081
  • GL50803_41701
  • THAPSDRAFT_264441
  • spyA
  • Ogt
Protein Region
Peptide Type
Blocking Peptide (BP)
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Specificity The synthetic peptide sequence used to generate the antibody AP6695b was selected from the C-term region of human OGT. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Background O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) 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 nine tetratricopeptide repeats and a putative bipartite nuclear localization signal.
Restrictions For Research Use only
Storage 4
Storage Comment Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Expiry Date 6 months
Background publications Fujiki, Chikanishi, Hashiba, Ito, Takada, Roeder, Kitagawa, Kato: "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis." in: Nature, Vol. 459, Issue 7245, pp. 455-9, 2009 (PubMed).

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, Vol. 284, Issue 6, pp. 3425-32, 2009 (PubMed).

Slawson, Lakshmanan, Knapp, Hart: "A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin." in: Molecular biology of the cell, Vol. 19, Issue 10, pp. 4130-40, 2008 (PubMed).