Analytical Data
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Gene name
OGT
- Application
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Alternative Names
O-GlcNAc transferase subunit p110O-linked N-acetylglucosamine transferase 110KDA subunit ;OGT
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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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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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
Related Products
Protein Description
OGT (O-GlcNAc transferase) is an essential enzyme that plays a critical role in the post-translational modification of proteins through the addition of O-Linked N-Acetylglucosamine (O-GlcNAc) residues. This modification is significant in cellular signaling, metabolism, and stress response, influencing various biological processes such as gene expression and cell differentiation. The dysregulation of OGT has been implicated in numerous diseases, including cancer, diabetes, and neurodegenerative disorders. Therefore, understanding the structure and function of OGT, as well as the mechanisms underlying its enzymatic activity, is crucial for developing potential therapeutic strategies. Recent advances in techniques such as X-ray crystallography and mass spectrometry have enhanced our ability to study OGT and its interactions with substrates and other cellular factors. Furthermore, the development of specific inhibitors and modulators of OGT is a promising area of research, which could pave the way for novel interventions in OGT-related diseases. Increasing evidence suggests that OGT's role as a molecular sensor linking nutrient availability to protein function is fundamental in maintaining cellular homeostasis, underlining the importance of continued investigation into this multifaceted enzyme.
