Found 2 discussions for this experiment
1 year ago
1 year ago by Christos Karampelas
I am currently using a recombinant protein which shows metal-dependent DNase activity. Is it possible to pinpoint the source of the DNase activity after protein purification? More specifically, can I ensure that the DNase activity is not because of nuclease contamination from the E.coli that might have persisted and passed with the protein of interest during purification?
3 years ago
3 years ago by Hollie Fowler
I am using 8M Urea to lyse my cells but after centrifugation my pellet is very viscous. This causes me trouble when I try to collect the supernatant. Is there any way to avoid it and do you think it will have an effect on the concentration of my protein?
Found 4 matching solutions for this experiment
|- Capable of extracting bacterial microcompartments (BMCs).|
|- The manufacturer protocol was followed.|
|- Compatible with most downstream workflows such as electrophoresis, affinity purification, immunoprecipitation, protein interaction analysis, crosslinking and protein labeling.|