- Antibody Type
- Recombinant monoclonal
- Target
- O-GlcNAc
- Reactivity
- Human,Mouse,Rat
- Application
- WB, IHC, IF, ELISA
- MW(Calculated)
- Multiple
- MW(Observed)
- Multiple
- Host Species
- Rabbit
- Isotype
- IgG, Kappa
- Conjugate
- Unconjugated
- Modification
- O-GlcNAcylation
- Modification Site
- Ser(S) /Thr (T)
- Recommended dilution ratio
- WB 1:200-1:1000;IF 1:200-1:1000;ELISA 1:5000-1:20000
- Composition
- PBS, 50 % Glycerol, 0.05% BSA, 0.05% Proclin 300
- Purification process
- Recombinant Antibody expressed in animal component-free (ACF) media, purified via Protein A affinity chromatography
- storageCondition
- -15°C to -25°C/1 year (Do not lower than -25°C)
- Stability
- Stable for 12 months from date of receipt / reconstitution.
- Concentration
- --
- Clonal
- Recombinant monoclonal
- Clone Number
- W-R7
- Immunogen
- polypeptide
- Gene Name
- --
- Protein Name
- --
- Alternative name
- --
- Organism-1
- --
- Gene ID
- --
- SwissProt-1
- --
- --
- Background:
- Background
- O-GlcNAc (short for O-linked β-N-acetylglucosamine) is a reversible enzymatic post-translational modification found on serine and threonine residues of nucleocytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N-acetylglucosamine (GlcNAc).It is widely involved in the regulation of diverse cellular processes, including transcription, cell cycle, signal transduction, and stress response. Dysregulation of O-GlcNAcylation has been closely linked to cancer, neurodegeneration, diabetes, and inflammatory diseases. Notably, elevated O-GlcNAc levels in many cancers have been reported to suppress apoptosis by inhibiting caspase activation.
- Cellular Localization
- O-GlcNAc is a post-translational modification involving the addition of a single N-acetylglucosamine moiety to the serine or threonine residues of nuclear and cytoplasmic proteins.
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- Background:O-GlcNAc (short for O-linked β-N-acetylglucosamine) is a reversible enzymatic post-translational modification found on serine and threonine residues of nucleocytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N-acetylglucosamine (GlcNAc).It is widely involved in the regulation of diverse cellular processes, including transcription, cell cycle, signal transduction, and stress response. Dysregulation of O-GlcNAcylation has been closely linked to cancer, neurodegeneration, diabetes, and inflammatory diseases. Notably, elevated O-GlcNAc levels in many cancers have been reported to suppress apoptosis by inhibiting caspase activation.
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