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Citations & References (7)
Invitrogen™
Click-IT™ O-GlcNAc Enzymatic Labeling System
The Click-iT™ O-GlcNAc Enzymatic Labeling System provides a highly sensitive and efficient method for the in-vitro modification of O-GlcNAc modifiedRead more
| Catalog Number | Quantity |
|---|---|
| C33368 | 1 Kit |
Catalog number C33368
Price (TWD)
***
Quantity:
1 Kit
Price (TWD)
***
The Click-iT™ O-GlcNAc Enzymatic Labeling System provides a highly sensitive and efficient method for the in-vitro modification of O-GlcNAc modified proteins. Proteins are enzymatically labeled utilizing the permissive mutant β-1,4-galactosyltransferase (Gal-T1 (Y289L)) which transfers azido-modified galactose (GalNAz) from UDP-GalNAz to O-GlcNAc residues. Then, via the chemoselective ligation or click reaction between an azide and an alkyne, the azido-labeled glycoproteins can then be detected with a Click-iT™ Glycoprotein Detection kit for gels (TAMRA or Dapoxyl™ alkyne) or Western blots (biotin alkyne). Labeling and detection can be completed in less than 24 hours and the Click-iT™ glycoprotein products are compatible with LC-MS/MS and Multiplexed Proteomics™ technologies for in-depth analyses of this important post-translational modification.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodBiotin-based, Fluorescence
Product LineClick-iT
Product TypeO-GlcNAc Enzymatic Labeling System
Quantity1 Kit
Shipping ConditionWet Ice
Labeling TargetProteins
Label or DyeAlexa Fluor 488, Alexa Fluor 555, Alexa Fluor 594, Alexa Fluor 647, Biotin, Oregon Green 488, TMR (Tetramethylrhodamine)
Unit SizeEach
Contents & Storage
Store in refrigerator at 2°C to 8°C
Citations & References (7)
Citations & References
Abstract
Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
Journal:Mol Cell Proteomics
PubMed ID:17507370
'O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli. O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation. A systematic glycoproteomics analysis of the affects of inhibiting
Novel in vivo-degradable cellulose-chitin copolymer from metabolically engineered Gluconacetobacter xylinus.
Journal:Appl Environ Microbiol
PubMed ID:20656868
'Despite excellent biocompatibility and mechanical properties, the poor in vitro and in vivo degradability of cellulose has limited its biomedical and biomass conversion applications. To address this issue, we report a metabolic engineering-based approach to the rational redesign of cellular metabolites to introduce N-acetylglucosamine (GlcNAc) residues into cellulosic biopolymers during
Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins.
Journal:J Am Chem Soc
PubMed ID:18683930
'We report an advanced chemoenzymatic labeling strategy for direct fluorescence detection of O-GlcNAc proteins in gels that facilitates proteomic studies and greatly extend the reach of existing technologies. These new tools also enable the expression and dynamics of O-GlcNAc modifications to be monitored by imaging in cells and tissues.
The chemical neurobiology of carbohydrates.
Journal:Chem Rev
PubMed ID:18452339
The problems associated with oligosaccharide analysis have hindered efforts to understand the biology of oligosaccharides yet have given chemists a unique opportunity to develop new methods to overcome these challenges. The development of chemical tools for the analysis of glycan structure and function is essential to advance our understanding of
O-linked N-acetylglucosamine modification on CCAAT enhancer-binding protein beta: role during adipocyte differentiation.
Journal:J Biol Chem
PubMed ID:19478079
CCAAT enhancer-binding protein (C/EBP)beta is a basic leucine zipper transcription factor family member, and can be phosphorylated, acetylated, and sumoylated. C/EBPbeta undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation on Thr(188) by MAPK or cyclin A/cdk2 primes the phosphorylations on Ser(184)/Thr(179) by GSK3beta, and these phosphorylations are required for the