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Key Documents

N0790

Sigma-Aldrich

NDSB 221

≥97% (TLC)

Synonym(s):

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

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About This Item

Empirical Formula (Hill Notation):
C9H19NO3S
CAS Number:
160788-56-7
Molecular Weight:
221.32
UNSPSC Code:
12161900
NACRES:
NA.25

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
GHS05

signalword

Danger

hcodes

H314

Hazard Classifications

Skin Corr. 1B

Storage Class

8A - Combustible corrosive hazardous materials

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
MKCS7039
MKCM9326
MKCM7512
MKCM5885
MKCG7617

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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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