Dear Prem,

an alternative method for you could try is LigandTracer. With this technology you spot your protein on a regular petri dish and have your other protein labelled (with a fluorphore or radionuclide) in solution. You can then follow the binding of the lablled protein to the spotted protein in real-time and thereby determine the affinity and binding kinetics, as illustrated in this article: Article SPECT imaging of distribution and retention of a brain-penet...

You can also use LigandTracer to study how the virus interacts with the host cells, as described in the following paper: Article Adenovirus with Hexon Tat-Protein Transduction Domain Modifi...

Thank you very much for sharing the posts

Hi Prem,

If you want to try in mammalian system, then here's one option-- CheckMate from PROMEGA: https://www.promega.com/products/protein-interactions/pulldown-and-two-hybrid-systems/checkmate-mammalian-two_hybrid-system/?catNum=E2440

There is SUS, but I think it's again in yeast. Halotag is a third option which keeps evolving over time, so please take a look at that as well.

Anoop

Hi Prem,

Co-immunoprecipitation (Co-IP) is a commonly used method to indirectly identify protein interactions. You can also use the co-expression and determine whether a complex is formed by the position of the elution peak from the gel filtration column. There are also high-throughput interaction screening methods such as phage display technology, interaction intensity and kinetic assays such as ITC and SPR. If you need to understand specific interaction interfaces you can use structural biology techniques. Creative Biostructure, experts in the field of structural biology, also offers solutions for verifying protein interactions.

https://www.creative-biostructure.com/protein-interaction-analysis-544.htm