Product Details

Purity

>85% (SDS-PAGE)

Target Names

Ogt

Uniprot No.

P56558

Alternative Names

Ogt; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; EC 2.4.1.255; O-GlcNAc transferase subunit p110; O-linked N-acetylglucosamine transferase 110 kDa subunit; OGT

Species

Rattus norvegicus (Rat)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

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). Has 3 distinct KM values for UDP-GlcNAc; GlcNAc concentration modulates its affinity for different substrates. 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.

Gene References into Functions

These findings indicate that oxidative environment promotes O-GlcNAcylation in skeletal muscle and suggest an interrelationship between cellular redox state and O-GlcNAc protein modificatio PMID: 25416863
Findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability. PMID: 24995978
protein O-GlcNAcylation, OGT, and OGA in the rat brain at various ages from embryonic day 15 to the age of 2 years PMID: 22928023
results suggest that cultured podocytes possess limited ability to synthesize glucosamine (GlcN) internally and therefore may need to receive GlcN from the extracellular environment. PMID: 20506529
Purification of a glycosylated protein p135, and it's identification as a O-GlcNAc transferase PMID: 11700029
the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its tetratricopeptide repeat protein-protein interaction domains PMID: 12724313
examined the characteristics and subcellular distribution of OGT protein and OGT activity and relationship to O-linked glycosylation; cytosolic OGT activity is 10 times more abundant in brain tissue compared with muscle, adipose, heart, and liver PMID: 12911634
The 26S proteasome can be inhibited by modification with the enzyme, O-GlcNAc transferase (OGT), thus inhibiting the proteolysis of transcription factor Sp1 and a hydrophobic peptide through inhibition of ATPase activity. PMID: 14675536
O-GlcNAc transferase binds to protein phosphatase 1 catalytic subunits PMID: 15247246
Neurodegenerative disease protein ataxin-10 (Atx-10) is associated with cytoplasmic O-linked beta-N-acetylglucosamine transferase in in the brain PMID: 16714295
These data support the notion that O-GlcNAc may play an important role as an internal stress response and that glucosamine-induced cardioprotection may be mediated via the p38 MAPK pathway. PMID: 17208994
Exerts pro-survival actions during hypoxia-reoxygenation in cardiac myocytes, particularly at the level of mitochondria. PMID: 18539296

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Subcellular Location

Cytoplasm. Nucleus. Cell membrane. Mitochondrion membrane. Cell projection.

Protein Families

Glycosyltransferase 41 family, O-GlcNAc transferase subfamily

Tissue Specificity

Expressed in brain, heart, liver, thymus, muscle, lung, spleen, uterus and ovary; in the kidney only an immunologically-related 78 kDa band is present, which is also present in liver and muscle. In the pancreas, expressed in both exocrine acinar cells and

Database Links

KEGG: rno:26295

STRING: 10116.ENSRNOP00000004692

UniGene: Rn.82705

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Recombinant Rat UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (Ogt), partial

Product Details

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