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40530

Sigma-Aldrich

Poly(ethylene glycol) octyl ether

Synonym(s):

C8En (n = 2 to 9), Polyethylene glycol, n-Octylpolyoxyethylene, Octyl-POE, Polyethylene glycol monooctyl ether, Rosenbusch-Tenside

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About This Item

Linear Formula:
CH3(CH2)6CH2(OCH2CH2)nOH
CAS Number:
27252-75-1
UNSPSC Code:
12161900
NACRES:
NA.25

form

liquid

refractive index

n20/D 1.452

InChI

1S/C10H22O2/c1-2-3-4-5-6-7-9-12-10-8-11/h11H,2-10H2,1H3

InChI key

ZQCIMPBZCZUDJM-UHFFFAOYSA-N

Related Categories

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H315,H319

Precautionary Statements

P305 + P351 + P338

Hazard Classifications

Eye Dam. 2

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

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Hester Emilie Hasper et al.
Biochemistry, 43(36), 11567-11575 (2004-09-08)
The peptide antibiotic nisin was the first reported example of an antibiotic that kills bacteria via targeted pore formation. The specific target of nisin is Lipid II, an essential intermediate in the bacterial cell-wall synthesis. High-affinity binding of the antibiotic
P J Mahasreshti et al.
Infection and immunity, 65(1), 211-218 (1997-01-01)
This study was conducted to partially characterize and identify the purity of two major outer membrane proteins (OMPs) (with molecular weights of 32,000 and 35,000 [32K and 35K, respectively]) of Pasteurella haemolytica. The 35K and 32K major OMPs, designated Pasteurella
Jesper E Mogensen et al.
Protein science : a publication of the Protein Society, 14(11), 2814-2827 (2005-10-04)
The adhesin involved in diffuse adherence (AIDA) is an autotransporter protein that confers the diffuse adherence phenotype to certain diarrheagenic Escherichia coli strains. It consists of a 49 amino acid signal peptide, a 797 amino acid passenger domain, and a
C Ostermeier et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(20), 10547-10553 (1997-10-06)
The aa3 type cytochrome c oxidase consisting of the core subunits I and II only was isolated from the soil bacterium Paracoccus denitrificans and crystallized as complex with a monoclonal antibody Fv fragment. Crystals could be grown in the presence
E V Yurkova et al.
Biomedical science, 1(6), 585-590 (1990-01-01)
The conditions for crystallization of the integral membrane protein bovine rhodopsin were determined. Crystals form over a wide range of protein concentration (0.4-15 mg ml-1) and pH (5.5-7.5) in detergent solutions of octyl-polyoxyethylene (o-POE) that contain inorganic salts as precipitants.

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