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Merck
CN

U5252

Sigma-Aldrich

尿苷 5′-二磷酸-N-乙酰半乳糖胺 二钠盐

≥97%, synthetic (organic), powder

别名:

UDP-N-乙酰半乳糖胺, 尿苷[5′]二磷酸[1]（2-乙酰氨基-2-脱氧 - α-D吡喃半乳糖） 二钠盐, 尿苷二磷酸半乳糖

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关于此项目

经验公式（希尔记法）:
C17H25N3Na2O17P2
化学文摘社编号:
108320-87-2
分子量:
651.32
Beilstein:
5375867
MDL编号:
MFCD00077894
UNSPSC代码:
41106305
PubChem化学物质编号:
24900653
NACRES:
NA.51

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产品名称

尿苷 5′-二磷酸-N-乙酰半乳糖胺 二钠盐, ≥97%

生物来源

synthetic (organic)

质量水平

200

方案

≥97%

表单

powder

溶解性

water: 50 mg/mL, clear, colorless

储存温度

−20°C

SMILES字符串

[Na+].[Na+].CC(=O)N[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OP([O-])(=O)OP([O-])(=O)OC[C@H]2OC([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O

InChI

1S/C17H27N3O17P2.2Na/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28;;/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28);;/q;2*+1/p-2/t7-,8-,10-,11+,12-,13-,14-,15?,16?;;/m1../s1

InChI key

HXWKMJZFIJNGES-QCVFHWOISA-L

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相关类别

一般描述

尿苷二磷酸(UDP)-GalNAc用作O-连接寡糖生物合成的前体。它还可作为甲壳素合成底物，甲壳素是真菌细胞壁以及节肢动物和昆虫外骨骼的主要成分。

应用

尿苷5′-二磷酸-N-乙酰半乳糖胺二钠盐已用作多肽N-乙酰半乳糖胺转移酶(ppGalNAc-T)的底物。

储存分类代码

11 - Combustible Solids

WGK

WGK 3

个人防护装备

dust mask type N95 (US), Eyeshields, Gloves

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
0000483352
0000483352
0000456603
0000456603
0000424364

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Inhibitor of ppGalNAc-T3-mediated O-glycosylation blocks cancer cell invasiveness and lowers FGF23 levels
Song L and Linstedt AD
eLife, 6, e24051-e24051 (2017)
UDP-sugar producing pyrophosphorylases--distinct and essential enzymes with overlapping substrate specificities, providing de novo precursors for glycosylation reactions
Decker D and Kleczkowski LA
Frontiers in Plant Science, 9, 1822-1822 (2018)
Xiaofei Guo et al.
Animals : an open access journal from MDPI, 8(10) (2018-09-23)
A new fecundity gene named the FecL (mutation), which regulates the ovulation rate, was discovered in French Lacaune sheep. The B4GALNT2 (beta-1, 4-N-acetyl-galactosaminyl transferase 2) gene was considered as the potential FecL mutation gene. This study explores whether the effect
Erandi Lira-Navarrete et al.
Nature communications, 6, 6937-6937 (2015-05-06)
Protein O-glycosylation is controlled by polypeptide GalNAc-transferases (GalNAc-Ts) that uniquely feature both a catalytic and lectin domain. The underlying molecular basis of how the lectin domains of GalNAc-Ts contribute to glycopeptide specificity and catalysis remains unclear. Here we present the
Kazuo Takahashi et al.
PloS one, 9(2), e99026-e99026 (2014-06-12)
Patients with IgA nephropathy (IgAN) have elevated circulating levels of IgA1 with some O-glycans consisting of galactose (Gal)-deficient N-acetylgalactosamine (GalNAc) with or without N-acetylneuraminic acid (NeuAc). We have analyzed O-glycosylation heterogeneity of naturally asialo-IgA1 (Ale) myeloma protein that mimics Gal-deficient
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