Datasheet

生物学的記述

Specificity	O-linked N-acetylglucosamine/O-GlcNAc Antibody (Mouse mAb) [B1J22] detects endogenous levels of total O-linked N-acetylglucosamine/O-GlcNAc protein.
Background	O‑linked N‑acetylglucosamine (O‑GlcNAc) is a dynamic monosaccharide modification added to serine and threonine residues of nuclear, cytoplasmic, and mitochondrial proteins by the single enzyme O‑GlcNAc transferase (OGT) and removed by O‑GlcNAcase (OGA), forming a two‑enzyme cycle that is tightly coupled to cellular nutrient status through the hexosamine biosynthetic pathway and UDP‑GlcNAc availability. The modification occurs on hundreds to thousands of regulatory proteins, including transcription factors, kinases, phosphatases, chromatin remodelers, cytoskeletal components, and metabolic enzymes, and often shares or flanks the same serine/threonine residues targeted by phosphorylation, creating reciprocal or cooperative O‑GlcNAc–phosphate “switches” that tune protein activity, subcellular localization, and interaction networks in response to glucose, amino acids, fatty acids, and stress signals. In signaling pathways, O‑GlcNAcylation modulates key nodes, including components of the insulin pathway, where elevated O‑GlcNAc on IRS‑1 and Akt interferes with their phosphorylation and attenuates downstream insulin signaling, linking chronic nutrient excess and increased flux through the hexosamine pathway to insulin resistance and type 2 diabetes phenotypes. On transcriptional and epigenetic regulation, OGT associates with chromatin at promoters and enhancers and modifies histones and transcriptional regulators, integrating nutrient cues into control of gene expression programs that affect cell growth, stress responses, and differentiation. In neurobiology, widespread O‑GlcNAcylation of neuronal proteins participates in synaptic function and proteostasis, and reductions in brain O‑GlcNAc, driven by regional glucose hypometabolism, correlate with increased phosphorylation and aggregation‑prone behavior of tau and other Alzheimer‑linked proteins; pharmacologic elevation of O‑GlcNAc on tau decreases its phosphorylation at disease‑relevant sites and alters its aggregation properties in experimental systems, identifying O‑GlcNAc cycling as a mechanistic link between metabolism and neurodegeneration. Dysregulated O‑GlcNAcylation is consistently associated with diabetes and its complications, cardiovascular dysfunction, cancer, and neurodegenerative disease.

Specificity

O-linked N-acetylglucosamine/O-GlcNAc Antibody (Mouse mAb) [B1J22] detects endogenous levels of total O-linked N-acetylglucosamine/O-GlcNAc protein.

Background

O‑linked N‑acetylglucosamine (O‑GlcNAc) is a dynamic monosaccharide modification added to serine and threonine residues of nuclear, cytoplasmic, and mitochondrial proteins by the single enzyme O‑GlcNAc transferase (OGT) and removed by O‑GlcNAcase (OGA), forming a two‑enzyme cycle that is tightly coupled to cellular nutrient status through the hexosamine biosynthetic pathway and UDP‑GlcNAc availability. The modification occurs on hundreds to thousands of regulatory proteins, including transcription factors, kinases, phosphatases, chromatin remodelers, cytoskeletal components, and metabolic enzymes, and often shares or flanks the same serine/threonine residues targeted by phosphorylation, creating reciprocal or cooperative O‑GlcNAc–phosphate “switches” that tune protein activity, subcellular localization, and interaction networks in response to glucose, amino acids, fatty acids, and stress signals. In signaling pathways, O‑GlcNAcylation modulates key nodes, including components of the insulin pathway, where elevated O‑GlcNAc on IRS‑1 and Akt interferes with their phosphorylation and attenuates downstream insulin signaling, linking chronic nutrient excess and increased flux through the hexosamine pathway to insulin resistance and type 2 diabetes phenotypes. On transcriptional and epigenetic regulation, OGT associates with chromatin at promoters and enhancers and modifies histones and transcriptional regulators, integrating nutrient cues into control of gene expression programs that affect cell growth, stress responses, and differentiation. In neurobiology, widespread O‑GlcNAcylation of neuronal proteins participates in synaptic function and proteostasis, and reductions in brain O‑GlcNAc, driven by regional glucose hypometabolism, correlate with increased phosphorylation and aggregation‑prone behavior of tau and other Alzheimer‑linked proteins; pharmacologic elevation of O‑GlcNAc on tau decreases its phosphorylation at disease‑relevant sites and alters its aggregation properties in experimental systems, identifying O‑GlcNAc cycling as a mechanistic link between metabolism and neurodegeneration. Dysregulated O‑GlcNAcylation is consistently associated with diabetes and its complications, cardiovascular dysfunction, cancer, and neurodegenerative disease.

使用情報

Application

WB, IP, IHC

Dilution

WB	IHC
1:1000	1:200

Reactivity

Chemical

Source

Mouse Monoclonal Antibody

MW

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/25336656/
https://pubmed.ncbi.nlm.nih.gov/30464755/

O-linked N-acetylglucosamine/O-GlcNAc Antibody (Mouse mAb) [B1J22]

生物学的記述

使用情報

References

Application Data