653600-61-4
Chemical Structure
UDP-GalNAz disodium
Synonym(s): UDP-N-azidoacetylgalactosamine disodium
- CAS No.: 653600-61-4
- Formula:C17H24N6Na2O17P2
- Molecular Weight:692.33
IUPAC Name: 2-bromo-6-chloroquinoline-4-carboxylic acid
InChIKey: XGTPLFSPWJKVQB-SGNQCPJASA-L
SMILES: O[C@H]1[C@@H](O)[C@H](N2C(NC(C=C2)=O)=O)O[C@@H]1COP(OP(O[C@@H]3[C@H](NC(CN=[N+]=[N-])=O)[C@@H](O)[C@@H](O)[C@@H](CO)O3)(O[Na])=O)(O[Na])=O
Biological Activity: UDP-GalNAz (UDP-N-azidoacetylgalactosamine) disodium is the analogue of UDP-GalNAc disodium (HY-114365). UDP-GalNAc disodium is the donor substrate of many N-acetylgalactosaminyltransferases, enzymes which transfer GalNAc from the nucleotide sugar to a saccharide or peptide acceptor. UDP-GalNAz disodium is a click chemistry reagent, it contains an Azide group and can undergo copper-catalyzed azide-alkyne cycloaddition reaction (CuAAc) with molecules containing Alkyne groups. It can also undergo strain-promoted alkyne-azide cycloaddition (SPAAC) reactions with molecules containing DBCO or BCN groups[1][2][3][4][5][6].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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UDP-GalNAz disodium | 99.89% | UDP-GalNAz (UDP-N-azidoacetylgalactosamine) disodium is the analogue of UDP-GalNAc disodium (HY-114365). UDP-GalNAc disodium is the donor substrate of many N-acetylgalactosaminyltransferases, enzymes which transfer GalNAc from the nucleotide sugar to a saccharide or peptide acceptor. UDP-GalNAz disodium is a click chemistry reagent, it contains an Azide group and can undergo copper-catalyzed azide-alkyne cycloaddition reaction (CuAAc) with molecules containing Alkyne groups. It can also undergo strain-promoted alkyne-azide cycloaddition (SPAAC) reactions with molecules containing DBCO or BCN groups. | ||||||||||||||||||||
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References
- [1]. Hang HC, et al. Probing glycosyltransferase activities with the Staudinger ligation. J Am Chem Soc. 2004;126(1):6-7. [Content Brief]
- [2]. Bourgeaux V, et al. Two-step enzymatic synthesis of UDP-N-acetylgalactosamine. Bioorg Med Chem Lett. 2005;15(24):5459-5462. [Content Brief]
- [3]. Hang HC, et al. A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. Proc Natl Acad Sci U S A. 2003;100(25):14846-14851. doi:10.1073/pnas.2335201100
- [4]. Lo PW, et al. O-GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2. Proc Natl Acad Sci U S A. 2018;115(28):7302-7307. [Content Brief]
- [5]. Vanessa Bourgeaux, et al. Two-step enzymatic synthesis of UDP-N-acetylgalactosamine. Bioorg Med Chem Lett. 2005 Dec 15;15(24):5459-62. [Content Brief]
- [6]. Choi J, et al., Engineering Orthogonal Polypeptide GalNAc-Transferase and UDP-Sugar Pairs. J Am Chem Soc. 2019 Aug 28;141(34):13442-13453. [Content Brief]
