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Human OGT O-Linked-N-Acetylglucosamine Transferase (ELISA Kit)

Human OGT O-Linked-N-Acetylglucosamine Transferase (ELISA Kit)

The Human OGT (O-Linked-N-Acetylglucosamine Transferase) ELISA Kit measures UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit in samples. The plate has been pre-coated with Human OGT antibody. OGT present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Human OGT Antibody is added and binds to OGT in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated OGT antibody. After incubation unbound Streptavidin-HRP is washed away during a washing step. Substrate solution is then added and color develops in proportion to the amount of Human OGT. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.

Catalog No: E6382Hu
Regular price $595.00 USD
Regular price $458.00 USD Sale price $595.00 USD
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2.5 weeks
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Product Details

Species Reactivity Human
Sensitivity 9.38 ng/L
Detection Range 20-4500 ng/L
Sample Type Serum, plasma, cell culture supernates
Incubation(s) 1.5 hour(s)
Research Areas Neuroscience, Signal Transduction
Background 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) (PubMed:26678539, PubMed:23103939, PubMed:21240259, PubMed:21285374, PubMed:15361863). 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 (PubMed:21285374). Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination (PubMed:26678539). 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 (By similarity). Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (PubMed:22923583). 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) (PubMed:22121020, PubMed:23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed:24474760). 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 (PubMed:12150998, PubMed:19451179, PubMed:20018868, PubMed:20200153, PubMed:21285374, PubMed:15361863). O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (PubMed:21285374, PubMed:28584052, PubMed:28302723). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Glycosylates HOXA1 (By similarity). O-glycosylates FNIP1 (PubMed:30699359). the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line. Source: UniProt Consortium (2025)
Shipping Condition Shipped on cold gel packs.
Storage Condition and Shelf Life 2-8C
Analyte UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Regulatory Status For Research Use Only
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