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C4695

Sigma-Aldrich

CHAPSO

BioXtra

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Synonym(s):
3-([3-Cholamidopropyl]dimethylammonio)-2-hydroxy-1-propanesulfonate
Empirical Formula (Hill Notation):
C32H58N2O8S
CAS Number:
Molecular Weight:
630.88
Beilstein:
5842642
MDL number:
PubChem Substance ID:
NACRES:
NA.25

description

zwitterionic

product line

BioXtra

Assay

≥98.0% (TLC)

form

powder

mol wt

micellar avg mol wt 7000

aggregation number

11

impurities

≤0.0005% Phosphorus (P)
≤0.1% Insoluble matter

ign. residue

≤0.1%

CMC

8 mM (20-25°C)
8 mM (micellar weight =9960)

mp

184-186 °C (lit.)

transition temp

cloud point 90 °C

solubility

H2O: 0.1 M, clear, colorless

anion traces

chloride (Cl-): ≤0.05%
sulfate (SO42-): ≤0.05%

cation traces

Al: ≤0.0005%
Ca: ≤0.0005%
Cu: ≤0.0005%
Fe: ≤0.0005%
K: ≤0.005%
Mg: ≤0.0005%
NH4+: ≤0.05%
Na: ≤0.01%
Pb: ≤0.001%
Zn: ≤0.0005%

SMILES string

[H][C@@]12C[C@H](O)CC[C@]1(C)[C@@]3([H])C[C@H](O)[C@]4(C)[C@]([H])(CC[C@@]4([H])[C@]3([H])[C@H](O)C2)[C@H](C)CCC(=O)NCCC[N+](C)(C)CC(O)CS([O-])(=O)=O

InChI

1S/C32H58N2O8S/c1-20(7-10-29(39)33-13-6-14-34(4,5)18-23(36)19-43(40,41)42)24-8-9-25-30-26(17-28(38)32(24,25)3)31(2)12-11-22(35)15-21(31)16-27(30)37/h20-28,30,35-38H,6-19H2,1-5H3,(H-,33,39,40,41,42)/t20-,21+,22-,23?,24-,25+,26+,27-,28+,30+,31+,32-/m1/s1

InChI key

GUQQBLRVXOUDTN-XOHPMCGNSA-N

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1 of 4

This Item
C3649220202220201
CHAPSO BioXtra

Sigma-Aldrich

C4695

CHAPSO

Premium Grade
CHAPSO ≥98%

Sigma-Aldrich

C3649

CHAPSO

-
CHAPSO Unique detergent with high CMC that solubilizes membrane-bound proteins in their native state.

Millipore

220202

CHAPSO

-
product line

BioXtra

product line

-

product line

-

product line

-

assay

≥98.0% (TLC)

assay

≥98%

assay

>98% (TLC)

assay

≥98% (NMR)

form

powder

form

powder

form

solid

form

crystalline powder

mol wt

micellar avg mol wt 7000

mol wt

micellar avg mol wt 7000

mol wt

micellar wt 9960

mol wt

micellar avg mol wt 6150

aggregation number

11

aggregation number

11

aggregation number

11

aggregation number

10

General description

Chapso is a zwitterionic detergent derived from Chaps by the addition of a functional hydroxyl group. It is a nondenaturing zwitterionic detergent with characteristics similar to CHAPS, although it is more soluble due to a more polar head group.

Application

Chapso has been used in a study to assess methods for high-throughput crystallization of membrane proteins. It has also been used in a study to investigate the effects of detergents on the structure of rhomboid proteases in a lipid environment.
A nondenaturing zwitterionic detergent with characteristics similar to CHAPS, although it is more soluble due to a more polar head group. Useful for the solubilization of integral membrane proteins.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Customers Also Viewed

Slide 1 of 2

1 of 2

Structure of Rhomboid Protease in a Lipid Environment
Vinothkumar, K., et al.
Journal of Molecular Biology, 407, 16-16 (2011)
Incomplete Dialysis of Protein Samples Containing 3-[(3-Cholamidopropyl)dimethylammonio]-1-propanesulfonate May Lead to Erroneous Estimation of Histidine Content on Amino Acid Analysis
Nomura, K., et al.
Analytical Biochemistry, 290, 4-4 (2001)
Satoko Osawa et al.
The Journal of biological chemistry, 283(28), 19283-19292 (2008-05-16)
gamma-Secretase is an aspartic protease that hydrolyzes type I membrane proteins within the hydrophobic environment of the lipid bilayer. Using the CHAPSO-solubilized gamma-secretase assay system, we previously found that gamma-secretase activity was sensitive to the concentrations of detergent and phosphatidylcholine.
Rachna Ujwal et al.
Methods (San Diego, Calif.), 55(4), 337-341 (2011-10-11)
Crystallization of membrane proteins remains a significant challenge. For proteins resistant to the traditional approach of directly crystallizing from detergents, lipidic phase crystallization can be a powerful tool. Bicelles are an excellent medium for crystallizing membrane proteins in a lipidic
Jonathan D J Wrigley et al.
Journal of neurochemistry, 90(6), 1312-1320 (2004-09-03)
Gamma-secretase performs the final processing step in the generation of amyloid-beta (Abeta) peptides, which are believed to be causative for Alzheimer's disease. Presenilins (PS) are required for gamma-secretase activity and the presence of two essential intramembranous aspartates (D257 and D385)

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