Date published: 2025-12-7

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O-GlcNAc transferase Substrates

Santa Cruz Biotechnology now offers a broad range of O-GlcNAc transferase Substrates for use in various applications. O-GlcNAc transferase (OGT) substrates are crucial in the study of protein glycosylation, a post-translational modification that involves the attachment of N-acetylglucosamine to serine and threonine residues on nuclear and cytoplasmic proteins. This modification is vital for regulating numerous cellular processes, including signal transduction, transcription, and protein-protein interactions. Researchers use OGT substrates to investigate the mechanisms of O-GlcNAcylation, exploring how this modification influences protein function, stability, and localization. Understanding O-GlcNAcylation is essential for explaining the broader implications of cellular metabolism, stress responses, and nutrient sensing, as these processes are tightly linked to the dynamic cycling of O-GlcNAc on proteins. The availability of specific OGT substrates enables scientists to conduct detailed studies on the enzyme's activity, substrate specificity, and regulatory mechanisms. Additionally, these substrates are used in the development of biochemical assays and analytical techniques for detecting and quantifying O-GlcNAc modifications, thereby advancing our knowledge of cellular homeostasis and signaling pathways. By providing a comprehensive range of OGT substrates, Santa Cruz Biotechnology supports cutting-edge research in the field of protein glycosylation, facilitating breakthroughs in our understanding of cellular regulation and its implications in various biological contexts. View detailed information on our available O-GlcNAc transferase Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

UDP-N-acetyl-D-glucosamine disodium salt

91183-98-1sc-286851
sc-286851A
sc-286851B
25 mg
100 mg
500 mg
$159.00
$424.00
$975.00
1
(1)

UDP-N-acetyl-D-glucosamine disodium salt serves as a critical substrate for O-GlcNAc transferase, facilitating the addition of O-GlcNAc moieties to serine and threonine residues on proteins. This modification plays a pivotal role in cellular signaling and regulation. The compound's structural features enable specific interactions with the enzyme's active site, influencing reaction kinetics and substrate specificity. Its dynamic participation in glycosylation pathways underscores its importance in cellular homeostasis and protein function modulation.