42131-42-0

Basic information

• Product Name: Poly(oxy-1,2-ethanediyl), alpha-(1-oxooctyl)-omega- hydroxy-, EO 3-10 mol
• Synonyms: Poly(oxy-1,2-ethanediyl), alpha-(1-oxooctyl)-omega- hydroxy-, EO 3-10 mol;Poly(oxy-1,2-ethanediyl), alpha-(1-oxooctyl)-omega-hydroxy-;Polyethylene glycol monocaprylate
• CAS NO: 42131-42-0
• Molecular Formula: C10H20O3
• Molecular Weight: 188.264
• Mol File: 42131-42-0.mol
• Article Data: 11

Chemical Properties

• Boiling Point: 288°Cat760mmHg
• Flash Point: 114.7°C
• Appearance: /
• Density: 0.967g/cm³
• Vapor Pressure: 0.000267mmHg at 25°C
• Refractive Index: 1.443
• CAS DataBase Reference: Poly(oxy-1,2-ethanediyl), alpha-(1-oxooctyl)-omega- hydroxy-, EO 3-10 mol(CAS DataBase Reference)
• NIST Chemistry Reference: Poly(oxy-1,2-ethanediyl), alpha-(1-oxooctyl)-omega- hydroxy-, EO 3-10 mol(42131-42-0)
• EPA Substance Registry System: Poly(oxy-1,2-ethanediyl), alpha-(1-oxooctyl)-omega- hydroxy-, EO 3-10 mol(42131-42-0)

Safety Data

• Hazardous Substances Data: 42131-42-0(Hazardous Substances Data)

Usage

InChI:InChI=1/C10H20O3/c1-2-3-4-5-6-7-10(12)13-9-8-11/h11H,2-9H2,1H3

Upstream product

• 497-26-7 2-methyl-1,3-dioxolane 
• 4359-57-3 2-heptyl-1,3-dioxolane 
• 107-21-1 ethylene glycol 
• 111-64-8 n-octanoic acid chloride 
• 124-07-2 Octanoic acid 
• 2615-15-8 pentaethylene glycol 
• 627-86-1 1,2-di-O-octanoyl-ethylene-glycerol 
• 107-07-3 2-chloro-ethanol 
• 124-12-9 caprylnitrile 

Relevant articles and documents

COMPOSITIONS COMPRISING ENZYME CLEAVABLE LINKER PLATFORMS AND CONJUGATES THEREOF

The present invention relates to a cleavable linker platform. In particular, the invention relates to construction of an enzyme cleavable linker platform conjugated to a drug or a diagnostically relevant compound, a biomolecule, and an enzyme cleavable group, for which cleavage of the enzyme cleavable group leads to release of the drug or diagnostically relevant compound.

Kinetics and quantitative structure-activity relationships for pseudomonas sp. Lipase-catalyzed hydrolysis of both monoesters and diesters of ethylene glycol

The goal of this work is to study kinetics and quantitative structure-activity relationships for steady states of Pseudomonas sp. lipase-catalyzed hydrolysis of both diesters and monoesters of ethylene glycol. Based on the steady-state kinetics of the enzyme-catalyzed hydrolysis of the diesters of ethylene glycol, the diesters and the monoesters react simultaneously as soon as monoester has started to build up in the reaction medium. In other words, the apparent Km values of the diesters are the Km values of the diesters (KmA) plus the Km values of the monoesters (KmB), and all Vmax values are about the same. Moreover, the pH-stat titration curve of the enzyme-catalyzed hydrolysis of the diesters of ethylene glycol is initially hyperbolic, then there is a sharp falloff in the hydrolysis rate. The abrupt stoppage of the reaction (relaxation stage) may be due to the existence of two phases in the reaction medium, that is, the product (ethylene glycol) and the substrates (the diesters of ethylene glycol) are not miscible. Furthermore, quantitative structure-activity relationships for varied acyl groups of mono- and diesters of ethylene glycol are studied. The fact that both pKmA and pK mB values are linearly correlated with the hydrophobicity constant (π) but not with the electronic substituent constants (σ*) indicates that the affinity of these substrates for the enzyme depends only on the hydrophobicitv of substrates. Copyright

Process for preventing consolidation of p-dichlorobenzene

A triethylene glycol derivative is added to p-dichlorobenzene so as to prevent consolidation and improve flowability of p-dichlorobenzene.