2-dodecoxyethanol

Conditions: temp:0.00; pressure:0.00; stir:; See reaction.notes.procedure_details.

Procedure: The FIG. 7 shows the results. The samples were loaded on the gels in the following order (from left to right) lane-1 control sample, lane 2-3 thiodiglycol, lane 4-5 Tween-20, lane 6-7 NP-40, lane 8-9 Brij-35, lane 10 SDS, lane 11 CHAPSO, 12-13 Triton-X100, lane 14 CHAP lane 15 control. The electrophoresis results shows (after a comparison of several typical runs) that, with exception of SDS and de-oxycholate treated protein samples, most protein samples containing detergent showed batch to batch variation in protein precipitation yield. The protein precipitation yield depended on the techniques used for harvesting the precipitated protein. There were occasions when the precipitation yield of duplicate samples varied between 100% to 50%. Protein samples containing SDS invariably showed substantially 100% yield in multiple tests.

Conditions: temp:0.00; pressure:0.00; stir:; See reaction.notes.procedure_details.

Procedure: The FIG. 7 shows the results. The samples were loaded on the gels in the following order (from left to right) lane-1 control sample, lane 2-3 thiodiglycol, lane 4-5 Tween-20, lane 6-7 NP-40, lane 8-9 Brij-35, lane 10 SDS, lane 11 CHAPSO, 12-13 Triton-X100, lane 14 CHAP and lane 15 control. The electrophoresis results shows (after a comparison of several typical runs) that, with exception of SDS and de-oxycholate treated protein samples, most protein samples containing detergent showed batch to batch variation in protein precipitation yield. The protein precipitation yield depended on the techniques used for harvesting the precipitated protein. There were occasions when the precipitation yield of duplicate samples varied between 100% to 50%. Protein samples containing SDS invariably showed substantially 100% yield in multiple tests.

Conditions: temp:0.00; pressure:0.00; stir:; See reaction.notes.procedure_details.

Procedure: To a 2 liter volumetric flask containing approximately 1500 ml. of distilled water is added 20.0 g. of sulfanilamide (0.116 mol), 66 ml. of Brij 35 and 200 ml. of concentrated hydrochloric acid. The resulting mixture is taken up to 2 liters with distilled water and then stirred until the sulfanilamide is completely dissolved. To a 2 liter volumetric flask containing approximately 1500 ml is completely dissolved

Conditions: temp:0.00; pressure:0.00; stir:; See reaction.notes.procedure_details.

Procedure: An Abl reaction mixture was prepared by mixing 1 ml of reaction buffer (50 mM Tris-HCl, 10 mM MgCl2 1 mM EGTA 2 mM dithiothreitol (pH 7.5 at 25° C.)), 10 μl of 10 mM ATP, 2 μl of 6-(9-oxo-9H-acridin-10yl) hexanoate-labelled Abl Peptide substrate (non-phosphorylated) (500 μM in DMSO). 100 μl of this mixture was placed into the wells of a black flat bottomed microtitre plate. The reaction was initiated by the addition of 10 μl of Abl kinase (New England Biolabs, Code P6050L Lot 5), (100,000 units/ml or 100 units/μl) which had been diluted in reaction buffer (50 mM Tris-HCl, 10 mM MgCl2, 1 mM EGTA, 2 mM dithiothreitol, 0.01% Brij 35 (pH 7.5 at 25° C.) to a concentration of 100 units per 10 μl. An Abl reaction mixture was prepared by mixing The reaction was initiated by the addition of 10 μl of Abl kinase (New England Biolabs, Code P6050L Lot 5), (100,000 units/ml or 100 units/μl) which