Analytical Data
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Gene name
OGT
- Application
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Alternative Names
OGT；UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15294
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Expression Region
606-1022aa
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AA Sequence
MAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQ
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Molecular Weight
62.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The study of OGT (O-GlcNAc transferase) recombinant protein is rooted in the understanding of O-GlcNAcylation, a vital post-translational modification that regulates numerous cellular processes including signal transduction, gene expression, and protein stability. OGT is the enzyme responsible for adding O-GlcNAc moieties to serine and threonine residues on target proteins, influencing their function and interactions. Dysregulation of O-GlcNAcylation has been implicated in various diseases, such as cancer, diabetes, and neurodegenerative disorders, highlighting the importance of OGT in maintaining cellular homeostasis. Developing recombinant forms of OGT facilitates in-depth studies of its enzymatic activity, substrate specificity, and its role in cellular signaling pathways. By producing OGT in a controlled laboratory environment, researchers aim to unravel the complex regulatory mechanisms of O-GlcNAcylation, explore potential therapeutic targets, and develop strategies to modulate OGT activity for disease intervention. This area of research not only advances our molecular understanding of cellular dynamics but also opens avenues for novel drug development aimed at mitigating the effects of OGT dysregulation in pathological conditions.
