ELISA Recombinant UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110KDA subunit(OGT),partial

Quantity: 200µg. Other Quantitys are also available. Please Inquire. In Stock: No Lead time: 10-20 working days Research Topic: Neuroscience Uniprot ID: O15294 Gene Names: OGT Organism: Homo sapiens () AA Sequence: MAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQ Expression Region: 606-1022aa Sequence Info: Partial Source: E.coli Tag Info: N-terminal 6xHis-SUMO-tagged MW: 62.5 kDa Alternative Name(s): O-GlcNAc transferase subunit p110O-linked N-acetylglucosamine transferase 110KDA subunit ;OGT Relevance: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in Cytoplasmic domain and nuclear proteins resµLting 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 regµLate their cellµLar processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insµLin resistance in muscle and adipocyte cells via glycosylating insµLin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insµLin signaling. Involved in glycolysis regµLation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regµLation 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 RegµLates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK throµgh 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 Reference: O-GlcNAcylation regµLates 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) Purity: Greater than 90% as determined by SDS-PAGE. Storage Buffer: Tris-based buffer，50% glycerol Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.