Recombinant Human Udp-N-Acetylglucosamine--Peptide N-Acetylglucosaminyltransferase 110 Kda Subunit (OGT) Protein (His-SUMO)

Name: Recombinant Human Udp-N-Acetylglucosamine--Peptide N-Acetylglucosaminyltransferase 110 Kda Subunit (OGT) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09872P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Udp-N-Acetylglucosamine--Peptide N-Acetylglucosaminyltransferase 110 Kda Subunit (OGT) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O15294
Target Symbol	OGT
Synonyms	FLJ23071; GlcNAc transferase; HRNT1; MGC22921; O GlcNAc; O GlcNAc transferase p110 subunit ; O GlcNAc transferase subunit p110; O linked N acetylglucosamine (GlcNAc) transferase (UDP N acetylglucosamine:polypeptide N acetylglucosaminyl transferase); O linked N acetylglucosamine (GlcNAc) transferase; O linked N acetylglucosamine transferase 110 kDa subunit; O-GlcNAc transferase subunit p110; O-linked N-acetylglucosamine transferase 110 kDa subunit; ogt; OGT1_HUMAN; UDP N acetylglucosamine peptide N acetylglucosaminyltransferase 110 kDa subunit; UDP N acetylglucosamine peptide N acetylglucosaminyltransferase GlcNAc transferase; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase; Uridinediphospho N acetylglucosamine:polypeptide beta N acetylglucosaminyl transferase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQ
Expression Range	606-1022aa
Protein Length	Partial
Mol. Weight	62.5kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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). 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. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination. 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. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. 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). 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. 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. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity. Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1. Glycosylates HOXA1. O-glycosylates FNIP1.; the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.
Subcellular Location	Nucleus. Cytoplasm.; [Isoform 2]: Mitochondrion. Membrane.; [Isoform 3]: Cytoplasm. Nucleus. Cell membrane. Mitochondrion membrane. Cell projection.; [Isoform 4]: Cytoplasm. Nucleus.
Protein Families	Glycosyltransferase 41 family, O-GlcNAc transferase subfamily
Database References	HGNC: 8127 OMIM: 300255 KEGG: hsa:8473 STRING: 9606.ENSP00000362824 UniGene: Hs.405410
Associated Diseases	Mental retardation, X-linked 106 (MRX106)
Tissue Specificity	Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver.

Gene Functions References

High OGT expression is associated with breast cancer. PMID: 30106436
O-GlcNAc transferase (OGT) is a partner of the MCM2-7 complex and O-GlcNAcylation might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions. PMID: 30069701
LXRalpha interacts with OGT in its N-terminal domain and ligand-binding domain (LBD) in a ligand-independent fashion. PMID: 29577901
Findings demonstrate a novel role of Poleta O-GlcNAcylation by OGT in translesion DNA synthesis regulation and genome stability maintenance. PMID: 29208956
OGT, a unique glycosyltransferase enzyme, was identified to be upregulated in non-alcoholic fatty liver disease-associated hepatocellular carcinoma tissues by transcriptome sequencing. Here, we found that OGT plays a role in cancer by promoting tumor growth and metastasis in cell models. This effect is mediated by the induction of palmitic acid. PMID: 28347804
Nrf1 is regulated by O-GlcNAc transferase. PMID: 28625484
Findings indicate O-linked N-acetylglucosamine transferase (OGT) as a cellular factor involved in human papillomaviruses type 16/18 E6 and E7 expressions and cervical cancer tumorigenesis, suggesting that targeting OGT in cervical cancer may have potential therapeutic benefit. PMID: 27331873
The findings suggest that OGT promotes the O-GlcNAc modification of HDAC1 in the development of progression hepatocellular carcinoma. PMID: 27060025
Tax interacts with the host OGT/OGA complex and inhibits the activity of OGT-bound OGA. PMID: 28742148
We identified two human PRC2 complexes and two PR-DUB deubiquitination complexes, which contain the O-linked N-acetylglucosamine transferase OGT1 and several transcription factors. PMID: 27705803
Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability PMID: 28584052
This work uncovers that URI-regulated OGT confers c-MYC-dependent survival functions in response to glucose fluctuations. PMID: 27505673
The results of this study showed that the OGT is essential for sensory neuron survival and target innervation. PMID: 28115479
The authors show that O-GlcNAcylation of KEAP1 by OGT at serine 104 is required for the efficient ubiquitination and degradation of NRF2. PMID: 28663241
Data suggest that O-GlcNAc transferase 1 (OGT1) specifically binds to, O-GlcNAcylates, and stabilizes nonspecific lethal protein3 (NSL3); stabilization of NSL3 by OGT1 up-regulates global acetylation levels of histone 4 at Lys-5, Lys-8, and Lys-16. PMID: 28450392
conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 stability. These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis. PMID: 28455227
Fatty acid synthase fine-tunes the cell's response to stress and injury by remodeling cellular O-GlcNAcylation PMID: 28232487
OGT functions in metastatic spread of HPV E6/E7-positive HeLa cells to xenografted lungs through E6/E7, HCF-1 and CXCR4 PMID: 27845045
Reducing endogenous mitochondrial OGT expression leads to alterations in mitochondrial structure and function, including Drp1-dependent mitochondrial fragmentation, reduction in mitochondrial membrane potential, and a significant loss of mitochondrial content in the absence of mitochondrial reactive oxygen species. PMID: 28100784
Thus, a single amino acid substitution in the regulatory domain (the tetratricopeptide repeat domain) of OGT, which catalyzes the O-GlcNAc post-translational modification of nuclear and cytosolic proteins, appears causal for X-linked intellectual disability. PMID: 28302723
Beyond its well-known role in adding beta-O-GlcNAc to serine and threonine residues of nuclear and cytoplasmic proteins, OGT also acts as a protease in the maturation of the cell cycle regulator, HCF-1, and serves as an integral member of several protein complexes, many of them linked to gene expression. (Review) PMID: 27294441
the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNAc-transferase (OGT) and O-GlcNAcase (OGA), interact with the (A)gamma-globin promoter at the -566 GATA repressor site PMID: 27231347
O-GlcNAcylation expression and its nuclear expression were associated with the carcinogenesis and progression of gastric carcinoma. PMID: 27131860
These results support a model in which OGT modifies HIRA to regulate HIRA-H3.3 complex formation and H3.3 nucleosome assembly and reveal the mechanism by which OGT functions in cellular senescence. PMID: 27217568
data indicate that O-GlcNAc-transferase activity is essential for RNA pol II promoter recruitment and that pol II goes through a cycling of O-GlcNAcylation at the promoter PMID: 27129214
OGT inhibited the formation of the Ecadherin/catenin complex through reducing the interaction between p120 and Ecadherin. PMID: 26707622
We concluded that OGT plays a key role in gastric cancer proliferation and survival, and could be a potential target for therapy. PMID: 26397041
Data suggest RNA polymerase II (POLR2A) is extensively modified on its unique C-terminal domain (CTD) by O-GlcNAc transferase (OGT); efficient O-GlcNAcylation requires a minimum of 20 heptad CTD repeats in POLR2A and more than half of NTD of OGT. PMID: 26807597
Together, these findings suggest that induction of SNO-OGT by Ab exposure is a pathogenic mechanism to cause cellular hypo-O-GlcNAcylation by which Ab neurotoxicity is executed PMID: 26854602
These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression. PMID: 26252736
These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity. PMID: 26305326
This work reveals that although the N-terminal TPR repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site specificity. PMID: 26237509
OGT expression is increased under hypoxic conditions. PMID: 26399441
E2F1 negatively regulates both Ogt and Mgea5 expression in an Rb1 protein-dependent manner. PMID: 26527687
a new function of histone O-GlcNAcylation in DNA damage response PMID: 26408091
Inhibition of O-Linked N-Acetylglucosamine Transferase Reduces Replication of Herpes Simplex Virus and Human Cytomegalovirus. PMID: 26041297
miR4235p was associated with congestive heart failure and the expression levels of proBNP; in addition, OGT was found to be a direct target of miR4235p. PMID: 25776937
Use of OGT(C917A) enhances O-GlcNDAz production, yielding improved cross-linking of O-GlcNDAz-modified molecules PMID: 26240142
Hexosamine biosynthetic pathway flux is increased in idiopathic pulmonary artery hypertension and drives OGT-facilitated pulmonary artery smooth muscle cell proliferation via specific proteolysis and direct activation of host cell factor-1. PMID: 25663381
Histone demethylase LSD2 acts as an E3 ubiquitin ligase and inhibits cancer cell growth through promoting proteasomal degradation of OGT. PMID: 25773598
Amino acid composition of splice variants, post-translational modifications, and stable associations with regulatory proteins influence subcellular distribution/substrate specificity of OGT and OGA (O-GlcNAcase beta-N-acetylglucosaminidase). [REVIEW] PMID: 25173736
Endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites. PMID: 24580054
Phosphorylation of TET proteins is regulated via O-GlcNAcylation by the O-linked N-acetylglucosamine transferase (OGT). PMID: 25568311
O-linked beta-N-acetylglucosamine transferase mediates O-GlcNAcylation of the SNARE protein SNAP-29 and regulates autophagy in a nutrient-dependent manner. PMID: 25419848
Instead, an adipogenesis-dependent increase in O-linked beta-N-acetylglucosamine (O-GlcNAc) glycosylation of EWS was observed. PMID: 24928395
Estrogen replacement therapy and plyometric training influence muscle OGT and OGA gene expression, which may be one of the mechanisms by which HRT and PT prevent aging-related loss of muscle mass. PMID: 24365779
OGT catalyzes the O-GlcNAcylation of TET3, promotes TET3 nuclear export, and, consequently, inhibits the formation of 5-hydroxymethylcytosine catalyzed by TET3. PMID: 24394411
Data suggest that with multi-substrate enzymes, such as OGT, specific inhibition can rarely be achieved with ligands that compete solely with one of the substrates; OGT is inhibited by bisubstrate UDP-oligopeptide conjugates. PMID: 24256146
The backbone carbonyl oxygen of Leu653 and the hydroxyl group of Thr560 in OGT contribute to the recognition of sugar moieties via hydrogen bonds. PMID: 23700425
Expression of c-MYC and OGT was tightly correlated in human prostate cancer samples. PMID: 23720054

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.