The Click-iT™ GalNAz metabolic glycoprotein labeling reagent provides the first part of a simple and robust two-step technique to identify자세히 알아보기
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카탈로그 번호
수량
C33365
5.2 mg
카탈로그 번호 C33365
제품 가격(KRW)
581,000
온라인 행사
Ends: 31-Mar-2026
683,000
할인액 102,000 (15%)
Each
카트에 추가하기
수량:
5.2 mg
제품 가격(KRW)
581,000
온라인 행사
Ends: 31-Mar-2026
683,000
할인액 102,000 (15%)
Each
카트에 추가하기
The Click-iT™ GalNAz metabolic glycoprotein labeling reagent provides the first part of a simple and robust two-step technique to identify and characterize cell surface O-linked glycoproteins. In step one, cultured cells are incubated with the azide-modified galactosamine (GalNAz). The azido-sugar is metabolically incorporated into cell surface O-linked glycoproteins through the permissive nature of the oligosaccharide biosynthesis pathway. In step two, 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). These Click-iT™ products are compatible with LC-MS⁄MS and Multiplexed Proteomics™ technologies for in-depth analyses of the glycoproteome.
For Research Use Only. Not for use in diagnostic procedures.
사양
검출 방법Biotin-based, Fluorescence
그린 기능Less hazardous
제품라인Click-iT
제품 유형Labeling Reagent
수량5.2 mg
배송 조건Room Temperature
Labeling TargetProteins
라벨 또는 염료Alexa Fluor 488, Alexa Fluor 555, Alexa Fluor 594, Alexa Fluor 647, Biotin, Oregon Green 488, TMR (Tetramethylrhodamine)
Unit SizeEach
구성 및 보관
Store in freezer -5°C to -30°C.
인용 및 참조 문헌 (5)
인용 및 참조 문헌
Abstract
Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor alpha depends on specific sialylated O-linked glycans on gB.
Authors:Wang J, Fan Q, Satoh T, Arii J, Lanier LL, Spear PG, Kawaguchi Y, Arase H,
Journal:J Virol
PubMed ID:19812165
'Paired immunoglobulin-like type 2 receptor alpha (PILRalpha) is an inhibitory receptor expressed on both hematopoietic and nonhematopoietic cells. Its binding to a cellular ligand, CD99, depends on the presence of sialylated O-linked glycans on CD99. Glycoprotein B (gB) of herpes simplex virus type 1 (HSV-1) binds to PILRalpha, and this ... More
Metabolic labeling of glycans with azido sugars for visualization and glycoproteomics.
Authors:Laughlin ST, Agard NJ, Baskin JM, Carrico IS, Chang PV, Ganguli AS, Hangauer MJ, Lo A, Prescher JA, Bertozzi CR,
Journal:Methods Enzymol
PubMed ID:17116478
'The staggering complexity of glycans renders their analysis extraordinarily difficult, particularly in living systems. A recently developed technology, termed metabolic oligosaccharide engineering, enables glycan labeling with probes for visualization in cells and living animals, and enrichment of specific glycoconjugate types for proteomic analysis. This technology involves metabolic labeling of glycans ... More
The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase.
'Membrane-type 1 matrix metalloproteinase (MT1-MMP; MMP-14) drives fundamental physiological and pathological processes, due to its ability to process a broad spectrum of substrates. Because subtle changes in its activity can produce profound physiological effects, MT1-MMP is tightly regulated. Currently, many aspects of this regulation remain to be elucidated. It has ... More
Dynamic monitoring of newly synthesized proteomes: up-regulation of myristoylated protein kinase A during butyric acid induced apoptosis.
Authors:Liu K, Yang PY, Na Z, Yao SQ,
Journal:Angew Chem Int Ed Engl
PubMed ID:21678537
Doubly charged: A double metabolic incorporation approach capable of proteome-wide profiling of post-translational modification dynamics on newly synthesized proteins has been developed (see scheme; blue box: methionine surrogate, orange diamond: PTM probe). This strategy reveals for the first time that up-regulation of myristoylated PKA protein is necessary for the occurrence ... More
Sialic Acids Attached to O-Glycans Modulate Voltage-gated Potassium Channel Gating.
Authors:Schwetz TA, Norring SA, Ednie AR, Bennett ES,
Journal:J Biol Chem
PubMed ID:21115483
Neuronal, cardiac, and skeletal muscle action potentials are produced and conducted through the highly regulated activity of several types of voltage-gated ion channels. Voltage-gated potassium (K(v)) channels are responsible for action potential repolarization. Glycans can be attached to glycoproteins through N- and O-linkages. Previous reports described the impact of N-glycans ... More