| Chemical Properties | Back Directory | [storage temp. ]
4°C, away from moisture | [form ]
Solid | [color ]
White to off-white | [InChIKey]
DEMHLQMPXSOKPT-ZVAGGMMLNA-N | [SMILES]
O[C@@H]1[C@@H]([C@@H](COP(O)(=O)OP(O)(=O)O[C@H]2O[C@H](CO)[C@H](O)[C@H](O)[C@H]2NC(=O)CN=[N+]=[N-])O[C@H]1N1C=CC(=O)NC1=O)O.[NaH] |&1:1,2,3,14,16,19,21,23,32,r| |
| Hazard Information | Back Directory | [Uses]
UDP-GalNAz disodium (UDP-N-azidoacetylgalactosamine disodium) is the analogue of UDP-GalNAc. UDP-GalNAc is the donor substrate of many N-acetylgalactosaminyltransferases, enzymes which transfer GalNAc from the nucleotide sugar to a saccharide or peptide acceptor[1]. 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. | [Biological Activity]
UDP-GalNAz disodium (UDP-N-azidoacetylgalactosamine disodium) is the analogue of UDP-GalNAc. UDP-GalNAc is the donor substrate of many N-acetylgalactosaminyltransferases, enzymes which transfer GalNAc from the nucleotide sugar to a saccharide or peptide acceptor[1]. | [storage]
4°C, away from moisture | [References]
[1]. Hang HC, et al. Probing glycosyltransferase activities with the Staudinger ligation. J Am Chem Soc. 2004;126(1):6-7. [2]. Bourgeaux V, et al. Two-step enzymatic synthesis of UDP-N-acetylgalactosamine. Bioorg Med Chem Lett. 2005;15(24):5459-5462. [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. [5]. Vanessa Bourgeaux, et al. Two-step enzymatic synthesis of UDP-N-acetylgalactosamine. Bioorg Med Chem Lett. 2005 Dec 15;15(24):5459-62. |
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