O-GlcNAc transferase Antibody (C-10) is a mouse monoclonal IgG2a (lambda light chain) provided at 200 µg/ml
specific for an epitope mapping between amino acids 927-961 within an internal region of O-GlcNAc transferase of human origin
recommended for detection of O-GlcNAc transferase of mouse, rat, human and avian origin by WB, IP, IF, IHC(P) and ELISA; also reactive with additional species, including and equine, canine, bovine, porcine and avian
blocking peptide, sc-376253 P
See m-IgGλ BP-HRP (mouse IgGλ binding protein-HRP), our highly recommended recombinant alternative to conventional secondary anti-mouse IgG reagents.
See O-GlcNAc transferase (F-12): sc-74546 for O-GlcNAc transferase antibody conjugates, including AC, HRP, FITC, PE, Alexa Fluor® 488, 594, 647, 680 and 790.
Every item is shipped based on the best shipping method assessed for the temperature requirements of that specific item. Items are grouped and shipped together whenever
possible, and a separate shipping charge will be included for each shipping method required. Shipping charges listed below are from our US warehouses to the Contiguous US,
Alaska, Hawaii, Canada and Puerto Rico. Shipping charges for countries outside the US and Canada will be determined once order has been received
Please note: We can not ship to PO boxes
Express Blue Ice
Express Dry Ice
Animal Health Prescription Item
SHIPPING METHODS & CHARGES
Ships via FedEx Ground to Contiguous US, Alaska, Canada, Monday through Friday. This method is used for less temperature sensitive items such as lab ware and animal
health products, bulky and/or heavy items
Labware ships FedEx Ground free of charge to the contiguous US
O-linked N-acetylglucosamine (O-GlcNAc) transferase (also designated 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. O-GlcNAc transferase has been purified from rat liver. It exists as a heterotrimeric complex with two subunits of the same molecular mass and one shorter subunit. Both polypeptides are related; the short subunit band is either a proteolytic product of the polypeptide or the product of an alternative translation start site. O-GlcNAc transferase is expressed as multiple transcripts that are present in different amounts in various human tissues, with the highest levels of expression in pancreas. Immunofluorescence of human cells expressing rat O-GlcNAc transferase indicated that it is present in both the nucleus and cytosol. HeLa cells expressing O-GlcNAc transferase do not survive well during prolonged incubations, suggesting that this protein may be toxic to the cells.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.