362000
N-羟乙酰神经氨酸
Formed by the action of CMP-Neu5Ac hydroxylase. Humans are devoid of this compound due to a mutation in the human CMP-Neu5Ac hydroxylase gene that occurred after the Homo-Pan divergence.
别名:
N-羟乙酰神经氨酸, 神经氨酸，N-羟乙酰神经氨酸
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关于此项目
经验公式（希尔记法）:
C11H19NO10
化学文摘社编号:
分子量:
325.27
UNSPSC Code:
12352201
NACRES:
NA.79
MDL number:
产品名称
N-羟乙酰神经氨酸, Formed by the action of CMP-Neu5Ac hydroxylase. Humans are devoid of this compound due to a mutation in the human CMP-Neu5Ac hydroxylase gene that occurred after the Homo-Pan divergence.
SMILES string
N([C@@H]([C@@H](O)[C@H](O)[C@H](O)CO)[C@@H](O)C(=O)C(=O)O)C(=O)CO
InChI
1S/C10H17NO10/c12-1-3(14)6(16)7(17)5(11-4(15)2-13)8(18)9(19)10(20)21/h3,5-8,12-14,16-18H,1-2H2,(H,11,15)(H,20,21)/t3-,5+,6-,7-,8-/m1/s1
InChI key
YIICUBSXBNCXHW-BOSCHMPASA-N
assay
≥98% (HPLC)
form
solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
color
off-white
solubility
water: 10 mg/mL
shipped in
ambient
storage temp.
−20°C
Quality Level
Disclaimer
毒性：标准处理（A）
General description
通过CMP-Neu5Ac羟化酶作用形成。除大脑外的类人猿组织的主要成分；然而，由于人CMP-Neu5Ac羟化酶基因中的突变（据报道，其在Homo-Pan分歧后发生），人类缺乏该化合物。
Other Notes
Chou, H.H., et al. 1998.Proc.Natl.Acad.Sci. USA 95, 11751.
Malykh, Y.N., et al. 1998.Glycoconj.J. 15, 885.
Malykh, Y.N., et al. 1998.Glycoconj.J. 15, 885.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
H H Chou et al.
Proceedings of the National Academy of Sciences of the United States of America, 95(20), 11751-11756 (1998-09-30)
Sialic acids are important cell-surface molecules of animals in the deuterostome lineage. Although humans do not express easily detectable amounts of N-glycolylneuraminic acid (Neu5Gc, a hydroxylated form of the common sialic acid N-acetylneuraminic acid, Neu5Ac), it is a major component
Y N Malykh et al.
Glycoconjugate journal, 15(9), 885-893 (1999-03-03)
The biosynthesis of the sialic acid N-glycolylneuraminic acid (Neu5Gc) occurs by the action of cytidine monophosphate-N-acetylneuraminate (CMP-Neu5Ac) hydroxylase. Previous investigations on a limited number of tissues suggest that the activity of this enzyme governs the extent of glycoconjugate sialylation with
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