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Merck
CN

N0790

NDSB 221

≥97% (TLC)

别名:

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

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关于此项目

经验公式(希尔记法):
C9H19NO3S
化学文摘社编号:
分子量:
221.32
NACRES:
NA.25
UNSPSC Code:
12161900
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description

zwitterionic

assay

≥97% (TLC)

form

solid

mol wt

221.32 g/mol

color

white

solubility

H2O: 50 mg/mL, clear, colorless

General description

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

Application

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.

Other Notes

This product is non-micelle forming.

pictograms

Corrosion

signalword

Danger

hcodes

Hazard Classifications

Skin Corr. 1B

存储类别

8A - Combustible corrosive hazardous materials

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies
Salvino S D'Amico and Georges G Feller
Analytical Biochemistry, 385, 3-3 (2009)
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)
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

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