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Citations & References (7)
Invitrogen™
Click-IT™ O-GlcNAc Enzymatic Labeling System
Click-iT™ O-GlcNAc酵素ラベリングシステムは、O-GlcNAc修飾タンパク質のin vitro修飾を行う高感度で効率的な手法を提供します。タンパク質は、UDP-GalNAz由来のアジド修飾ガラクトース（GalNAz）をO-GlcNAc残基に転写する透過性変異型、β-1,4-ガラクトシルトランスフェラーゼ（Gal-T1詳細を見る
| 製品番号（カタログ番号） | 数量 |
|---|---|
| C33368 | 1 Kit |
製品番号（カタログ番号） C33368
価格（JPY）お問い合わせください ›
45,000
Online offer
Ends: 27-Mar-2026
75,100割引額 30,100 (40%)
Each
数量:
1 Kit
Click-iT™ O-GlcNAc酵素ラベリングシステムは、O-GlcNAc修飾タンパク質のin vitro修飾を行う高感度で効率的な手法を提供します。タンパク質は、UDP-GalNAz由来のアジド修飾ガラクトース（GalNAz）をO-GlcNAc残基に転写する透過性変異型、β-1,4-ガラクトシルトランスフェラーゼ（Gal-T1（Y289L））を使用して酵素的に標識されます。その後は、アジドとアルキンの化学選択ライゲーションまたはクリック反応により、ゲル対応のClick-iT™糖タンパク質検出キット（TamraまたはDapoxyl™アルキン）またはウェスタンブロット（ビオチンアルキン）でアジド標識糖タンパク質を検出できます。標識と検出は24時間未満で完了できます。また、Click-iT™の糖タンパク質製品は、LC-MS/MSおよびMultiplexed Proteomics™技術と互換性があるため、重要な翻訳後修飾を詳細に分析できます。
研究用にのみ使用できます。診断用には使用いただけません。
仕様
検出法ビオチンベース、蛍光
製品ラインClick-iT
製品タイプO-GlcNAc酵素標識システム
数量1 Kit
出荷条件湿氷
Labeling Targetタンパク質
標識または色素Alexa Fluor 488, Alexa Fluor 555, Alexa Fluor 594, Alexa Fluor 647, ビオチン, Oregon Green 488, TMR（テトラメチルローダミン）
Unit SizeEach
組成および保存条件
冷蔵庫に2℃～8℃で保存
引用および参考文献 (7)
引用および参考文献
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