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Merck
CN
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主要文件

N0790

Sigma-Aldrich

NDSB 221

≥97% (TLC)

别名:

3-(1-Methylpiperidinio)-1-propanesulfonate, 3-(1-Methylpiperidinium)-1-propane sulfonate

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About This Item

经验公式(希尔记法):
C9H19NO3S
分子量:
221.32
UNSPSC代码:
12161900
NACRES:
NA.25

描述

zwitterionic

方案

≥97% (TLC)

表单

solid

分子量

221.32 g/mol

颜色

white

溶解性

H2O: 50 mg/mL, clear, colorless

一般描述

NDSB 221 is a nondetergent sulfobetaine that has been found to improve unfolding reversibility.

应用

NDSB 221 has been used in a study to identify a novel ligand binding site in phosphoserine phosphatase from Thermococcus onnurineus. It has also been used in a study to investigate its effects on acidic fibroblast growth factor (aFGF).
Non-detergent sulfobetaine is a compound used for non-denaturing protien purification. Increases the extraction yield of membrane, nuclear and cytoskeletal associated proteins. Zwitterionic over a wide pH range, easily removed by dialysis and no significant absorption in the near UV range. Specific applications include microsomal protein extraction, nuclear protein recovery, precipitation reduction in IEF, and membrane-bound protease purification. The typical usage concentration is 0.5 - 2.0 M.

其他说明

This product is non-micelle forming.

象形图

Corrosion

警示用语:

Danger

危险声明

危险分类

Skin Corr. 1B

储存分类代码

8A - Combustible corrosive hazardous materials

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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Long Xiang et al.
Journal of magnetic resonance (San Diego, Calif. : 1997), 194(1), 147-151 (2008-07-12)
Prevention of aggregation is critical for analyzing protein structure. Non-detergent sulfobetaines (NDSBs) are known to prevent protein aggregation, but the molecular mechanisms of their anti-aggregation effect are poorly understood. To elucidate the underlying mechanisms, we analyzed the effects of dimethylethylammonium
Identification of a novel ligand binding site in phosphoserine phosphatase from the hyperthermophilic archaeon Thermococcus onnurineus
Tae-Yang Jung et al.
Proteins: Structure, Function, and Genetics, 819-829 (2012)
A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies
Salvino S D'Amico and Georges G Feller
Analytical Biochemistry, 385, 3-3 (2009)

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