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

Name

O-Linked N-Acetylglucosamine (GlcNAc) Transferase (UDP-N-Acetylglucosamine:polypeptide-N-Acetylglucosaminyl Transferase) (OGT)
Synonyms HRNT1, FLJ23071, MGC22921, O-GLCNAC, MGC80426, MGC69550
Binding Site

C-Term
3 references available
Certificates ISO 9001:2008
Catalog no. ABIN696121
Quantity 0.1 mg
Price 49.50 $   Plus shipping costs $45.00
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Immunogen Synthetic peptide
Characteristics Blocking peptide for OGT (C-term) antibody ABIN390649
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.
Comments

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.

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Storage 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
Restrictions For Research Use only

Publications
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Product Slawson, Lakshmanan, Knapp et al.: "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).

Taylor, Geisler, Chambers et al.: "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).

Fujiki, Chikanishi, Hashiba et al.: "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis." in: Nature, Vol. 459, Issue 7245, pp. 455-9, 2009 (PubMed).