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Merck
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主要文件

M2925

Sigma-Aldrich

A3 Glycan

from bovine, ≥90% (HPLC)

别名:

(NeuNAc-Gal-GlcNAc)3Man3(GlcNAc)2, Mannotriose-di-(N-acetyl-D-glucosamine), tris(sialyl-galactosyl-N-acetyl-D-glucosaminyl)- ammonium salt, Trisialylated, galactosylated, triantennary N-glycan

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About This Item

经验公式(希尔记法):
C109H178N8O80
分子量:
2880.59
MDL號碼:
分類程式碼代碼:
12352201
NACRES:
NA.25

生物源

bovine

品質等級

化驗

≥90% (HPLC)

形狀

powder

儲存溫度

−20°C

一般說明

Many of the key molecules involved in the innate and adaptive immune response are glycoproteins

應用

A3 Glycan has been used in a study to assess the combination of two hydrophilic interaction chromatography methods that facilitate identification of 2-aminobenzamide-labeled oligosaccharides. It has also been used in a study to investigate glycan labeling strategies and their use in identification and quantification.

其他說明

To gain a comprehensive understanding of our extensive range of Polysaccharides for your research, we encourage you to visit our Carbohydrates Category page.

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves


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Göran Karlsson et al.
Journal of chromatographic science, 46(1), 68-73 (2008-01-26)
Hydrophilic interaction chromatography (HILIC) is used to separate 2-aminobenzamide- (2-AB) labeled N-linked oligosaccharides. The glycans of the model protein, bovine fetuin, are identified following comparison of elution patterns of seven 2-AB-labeled glycan standards, of which two are of the high-mannose
S Hunter Walker et al.
Journal of the American Society for Mass Spectrometry, 22(8), 1309-1317 (2011-09-29)
A library of neutral, hydrophobic reagents was synthesized for use as derivatizing agents in order to increase the ion abundance of N-linked glycans in electrospray ionization mass spectrometry (ESI MS). The glycans are derivatized via hydrazone formation and are shown

商品

N-连接聚糖、修饰和降解

N-linked glycosylation, modification, and degradation

N-linked glycosylation, modification, and degradation

N-linked glycosylation, modification, and degradation

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