Detergent Removal Reagents

The degradation and adsorption of 1-diazo-2-naphthol-4-sulfonic acid was studied using sewage sludge derived porous carbon . Application Involved in studies to analyze structure-activity relationships to predict biodegradability of N -heterocycles

NDSB-256 is a nondetergent sulfobetaines class member. Unlike CHAPS and other zwittergents, NDSBs are nondenaturing even at 1 M concentrations. NDSBs have been used to improve the efficiency of solubilization of membrane proteins, to isolate nuclear

NDSB-256 is a nondetergent sulfobetaines class member. Unlike CHAPS and other zwittergents, NDSBs are nondenaturing even at 1 M concentrations. NDSBs have been used to improve the efficiency of solubilization of membrane proteins, to isolate nuclear

Other Notes Ampholytic detergent used to enhance solubility of proteins in electrophoresis.

4&#8242-Methoxyacetophenone undergoes biocatalytic enantioselective reduction using immobilized Rhodotorula sp. AS2.

4&#8242-Methoxyacetophenone undergoes biocatalytic enantioselective reduction using immobilized Rhodotorula sp. AS2.

4&#8242-Methoxyacetophenone undergoes biocatalytic enantioselective reduction using immobilized Rhodotorula sp. AS2.

3-(4-heptyl)phenyl 3-hydroxypropyl dimethyl ammonio propane sulfonate (C7BzO) is a zwitterionic detergent comprising of a zwitterionic, hydrophilic head connected to the hydrophobic tail through a linker region. The prelinker region enhances

Multi-Enzymatic Cleaner, 1 Gal, 4/cs (27 cs/plt)

Crystal Clean consists of three separate components that when combined, serve to break the bond between the methamphetamine contaminant and the affected surface, allowing for easy removal. Crystal Clean is a commercial methamphetamine decontaminant

Detergent for the purification, extraction and solubilization of membrane-bound proteins in the native structure. It increases solubilization by dissociating aggregates and is easily removed by dialysis.

Detergent for the purification, extraction and solubilization of membrane-bound proteins in the native structure. It increases solubilization by dissociating aggregates and is easily removed by dialysis.