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Sigma-Aldrich

Poly(ethylenglycol)(18)-tridecylether

n=18, tridecyl ether group is a mixture of C11 to C14 iso-alkyl ethers with C13 iso-alkyl predominating

Synonym(e):

Polyoxyethylene (18) tridecyl ether

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About This Item

Lineare Formel:
C13H27(OCH2CH2)nOH, n~18
CAS-Nummer:
24938-91-8
MDL-Nummer:
MFCD00132049
UNSPSC-Code:
12162002
NACRES:
NA.23

Form

solid

Brechungsindex

n20/D 1.464 (lit.)

mp (Schmelzpunkt)

28 °C (lit.)

Hydroxylzahl

54‑62 mg KOH/g

Löslichkeit

water, isopropanol: 1 wt. % at 25 °C

Dichte

0.96 g/mL at 25 °C (lit.)

HLB

15

InChI

1S/C15H32O2/c1-2-3-4-5-6-7-8-9-10-11-12-14-17-15-13-16/h16H,2-15H2,1H3

InChIKey

OJDDJQYSKDIXOE-UHFFFAOYSA-N

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

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H Suzuki et al.
Journal of biochemistry, 93(3), 709-715 (1983-03-01)
The relationship between glucose metabolism and the "respiratory burst" of phagocytosing polymorphonuclear leukocytes (PMN) was studied in a Renex 30-treated cell system of guinea pig PMN by a polarometric technique. Phagocytosing PMN were treated with a detergent (Renex 30) and
M I Aveldaño
Archives of biochemistry and biophysics, 324(2), 331-343 (1995-12-20)
The solubilization of rhodopsin and phospholipids from disks prepared from bovine retinal rods was studied using five different detergents. The relative amounts of rhodopsin and lipid extracted during membrane solubilization differed dramatically with the nature of the surfactant; the two
J Giudicelli et al.
Biochimica et biophysica acta, 831(1), 59-66 (1985-09-20)
Neutral alpha-D-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) from horse kidney brush-border membranes was solubilized using Emulphogene BC 720 and purified by an affinity chromatography technique. The enzyme preparation (390-fold purified), which was free of other known microvillus hydrolases, exhibited one precipitate
Simultaneous demonstration of phagocytosis-connected oxygen consumption and corresponding NAD(P)H oxidase activity: direct evidence for NADPH as the predominant electron donor to oxygen in phagocytizing human neutrophils.
M Nakamura et al.
Biochemical and biophysical research communications, 98(3), 743-751 (1981-02-12)
T Shiibashi et al.
Developmental and comparative immunology, 25(5-6), 461-465 (2001-05-18)
NADPH oxidase has been identified as the superoxide-generating enzyme in fish neutrophils. To clarify the electron-donating ability of this enzyme, we examine the requirement of NADPH as the electron donor in superoxide generation in tilapia (Oreochromis niloticus) neutrophils using CLA-dependent
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