Found 2 discussions for this experiment
2 years ago
2 years 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?
4 years ago
4 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.
Fill out your contact details and receive price quotes in your InboxOutsource experiment