Mouse Monoclonal O-Linked N-Acetylglucosamine antibody - conjugated to Alexa Fluor® 647. Suitable for ICC/IF and reacts with Human samples.
IgG1
Mouse
Alexa Fluor® 647
Ex: 650nm, Em: 665nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Monoclonal
ICC/IF | |
---|---|
Human | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/200 | Notes This product gave a positive signal in MCF7 cells fixed with 4% formaldehyde (10 min) and 100% methanol (5 min). |
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Mouse Monoclonal O-Linked N-Acetylglucosamine antibody - conjugated to Alexa Fluor® 647. Suitable for ICC/IF and reacts with Human samples.
IgG1
Mouse
Alexa Fluor® 647
Ex: 650nm, Em: 665nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Monoclonal
RL2
IgG fraction
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle, Store in the dark
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This supplementary information is collated from multiple sources and compiled automatically.
O-Linked N-Acetylglucosamine (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. This dynamic modification is sometimes referred to as O-GlcNAcylation. The molecular mass of the O-GlcNAc group itself is approximately 203 Da. This modification is expressed widely across various tissues notably in the brain and pancreas. O-GlcNAc plays a critical role in regulating protein function stability and interaction.
O-GlcNAc modifies proteins influencing cellular processes such as transcription signal transduction and stress response. It is involved in the regulation of transcription factors like Sp1 and NF-kB and is associated with the O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) enzymes which respectively add and remove the GlcNAc group. O-GlcNAc functions in a manner similar to phosphorylation often competing with it on the same or adjacent serine/threonine sites. This modification is not part of a permanent protein complex but dynamically modulates protein interactions and activity.
This modification plays a fundamental role in pathways related to nutrient sensing and insulin signaling. It modulates proteins such as insulin receptor substrate 1 (IRS1) and Akt to link nutrient status to cellular responses. The hexosamine biosynthetic pathway (HBP) is an important pathway in which O-GlcNAc is synthesized. Through these pathways it impacts cellular signaling and metabolism influencing processes like cellular growth and apoptosis.
O-GlcNAc modification connects to conditions like diabetes and Alzheimer's disease. Elevated O-GlcNAc levels contribute to insulin resistance a hallmark of type 2 diabetes through interaction with proteins such as IRS1 and Akt. In Alzheimer's O-GlcNAc modifies tau protein reducing its phosphorylation and aggregation therefore potentially affecting neurofibrillary tangle formation. These connections underline the importance of O-GlcNAc in the pathophysiology of these diseases and highlight its potential as a therapeutic target.
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ab201994 staining O-Linked N-Acetylglucosamine in MCF7 cells. The cells were fixed with 4% formaldehyde (10 min), permeabilized with 0.1% Triton X-100 for 5 minutes and then blocked with 1% BSA/10% normal goat serum/0.3M glycine in 0.1% PBS-Tween for 1h. The cells were then incubated overnight at +4°C with ab201994 at 1/200 dilution (shown in red) and Alexa Fluor® 488 Anti-alpha Tubulin antibody [DM1A] - Microtubule Marker ab195887, Mouse monoclonal to alpha Tubulin (Alexa Fluor® 488), at 1/250 dilution (shown in green). Nuclear DNA was labelled with DAPI (shown in blue).
Image was taken with a confocal microscope (Leica-Microsystems, TCS SP8).
This product also gave a positive signal under the same testing conditions in MCF7 cells fixed with 100% methanol (5min).
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