Hi Sammy,
You can always try pull-down: you bind one enzyme to a purification column (bait) and run the target through, wash, and then elute, all while collecting small fractions of the flowthrough. You run your fractions on a gel and see if the target was retained by the bait and not washed out during the washes.
If you have access to a microscope you can try bi-molecular fluorescence complementation (BiFC)...
Hope this helps,
Anna
Hi,
Yes, many approaches exist please see here: . https://www.thermofisher.com/iq/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/overview-protein-protein-interaction-analysis.html
Good luck
Hi Sammy Pontrelli
I would suggest to first perform PLA suggested by Ondrej Havranek and if getting significant interaction then you may go for immunoprecipitation experiments. Both of them are simple and immunoprcipiation is very reliable for physical binding or interaction.
good luck
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