Polyethylene glycol tert-octylphenyl ether (Triton® X-114 substitute)

Polyethylene glycol tert-octylphenyl ether is a non-ionic detergent that is provided for research purposes or as a 10% proteomic grade solution. It is a substitute for Triton® X-114 (Triton® X-114 is registered trademark of Dow Chemical Company)

Proteomic Grade: DG009, DG010, DG509C, DG518C

Research Grade: 786-515, 786-516

Proteomic Grade Detergent Solutions

Many commercial grade detergents contain elevated levels of sulfhydryl oxidizing agents, peroxides, salts and carbonyl compounds. The proteins that are isolated with these detergents are highly susceptible to contaminating peroxides and carbonyls. The peroxides will oxidize proteins and the carbonyl groups will form Schiff’s bases with the proteins that interfere with its structure.   

G-Biosciences’ Proteomic Grade Detergent Solutions contain reduced peroxides and carbonyl compounds. In addition, the detergents have less than 50µS conductivity. These detergents are offered as sterile, 10% aqueous solutions, sealed under inert gas, and are suitable for protein applications. These non-ionic detergents are suitable for isolating membrane-protein complexes.   

Other Proteomic Grade Detergent Solutions offered include: Triton® X-100,Brij® 35, Brij® 58, Tween® 20, Tween® 80 and Nonidet® P-40 Substitute. A variety pack is also available, perfect for trial and optimization. The pack contains one 10ml vial of all seven proteomic grade detergents, as well as one gram samples of one of our Zwitterionic detergents (CHAPS) and one of our non-detergent sulfobetaines (NDSB 201).

Features

• Synonym: Polyethylene glycol tert-octylphenyl ether
• CAS Number: 9036-19-5
• Molecular Formula: C₁₄H₂₂O•[C₂H₄O]_7-8 for n =8
• Molecular Weight: ~537 (for n=7-8)
• Absorbance (254nm): 0.18 (0.05% w/v)
• Cloud Point: 23ºC
• Critical Micelle Concentration (CMC): approx 0.35 x 10^-3M (25ºC)

Applications

• A non-ionic detergent suitable for protein solubilization with phase-partitioning of hydrophilic proteins from amphiphilic proteins