If you are using magnetic beads, you don't need to do centrifugation. it would be separated by a magnet only. In the case of agarose beads, you would need centrifugation.

6 in-depth lecture slides couldn't help with what you did in 4 minutes! Thank you so much.

BEST EXPLANATION I'VE GOTTEN! THANK YOU!

Can you please explain how beta actin will be present in the lysates when we only pulled our protein of interest with the beads, all other proteins will be in the supernatant which we will discard or not use for this particular gel. We will run only those proteins which are in pellet and i think beta actin wont be presnt in pellet?

You save me! Really thank you Your video is precious!!

Lovely diagrams and nice clear explanation!

Very good explanation, thank you so much, and the diagrams are so neatly-drawn too! Was so confused about co-IP and IP before this haha. Thank you!

how do you justify the pH of the buffer to make sure that protein A and B are not dissociated?

hello! thank you very much for posting these explanations on youtube. just watched the long term potentiation (LTP) and this one about CO-IP and it helped me a lot! just subscribed :)

Great video! Super clear and easy to follow... I also liked your diagrams. Thanks for sharing

I don't understand why we need a second antibody for protein B! Would it not show anyway on the SDS Page? Or did I miss something?!

Thank you so much for the clear explanation! You saved my course!!!!

The difference between Pull-down and CoIp is that pull-down using solution from eluted beads, and CoIp uses the precipitate after centrifuge. Then both of them go to SDS-PAGE, is that right?

Do you pull down beta actin too with the beads? How do you get beta actin in an IP blot?

If we dont know which protein is interacted with Protein A then how we can use the antibody against the unknown protein. In this case we can only go for sequencing the SDS PAGE bands interacted with Protein A

thank you brother!

thanks a lot! from Argentina!!

Thank you so much for this clear explanation!

The best explanation l have found. Thank you

This was PERFECT! Thank you! Also you have very nice handwriting!

Lourd la vidéo, ça m'a mis bien 👍

Thanks a lot. your videos are really helpful for young researchers.

thanks this is short, concise and logical, made it easy to understand

4:53 how will you get any B-actin band from an immunoprecipitated sample? if b-actin is present this simply means that b-actin is also interacting with the protein A, which is WRONG!

Co-immunoprecipitation (Co-IP) is a popular technique to identify physiologically relevant protein-protein interactions by using target protein-specific antibodies to indirectly capture proteins that are bound to a specific target protein.

Explained very clearly thank you!

a very straightforward video ! thanks a lot !

Im a medical student,Thank you so much for this video❤️❤️❤️❤️it helps a lott!

Very useful and excellent explanation. Thanks a lot 👌

YOU SIR ARE GENIUS !

actin is used just to make sure the proteins you are testing presence for were loaded correctly on the blot?

It's fantastic thanks!

very helpful video, the only video explains co-IP with western blot!

Very nice presentation

Love your hand drawing!

Thank you man, it will facilitate my presentation. You are the best :))

Thanks for explanation! It was really helpful

Thank you for this video.

Where is protein A on the blot? How is A not blotted?

good job brah...keep uploading

thank you!

OH MY GOD THIS IS SO GOOD!!!!!!!!!!!!!!!!!!!! THANK YOU!!!!!!!!!!!!!

Super useful, thank you !!

Thanks

Do you have this information from a source? If so, which one? Can you send me the link please

So helpful, thanks!

Thanks for the very nice video. But I have a question. How can we detect unknown protein bound to the know protein in co immunoprecipitation ?

Thank you, sir :)

How we select antibody for a protein, How we can sure that our antibody interact with our protein??

thank you

Nicely explained explained. Could have been better if the importance of running input in the same gel was also given.

tell me are u from India? what is that accent??? i need to know

does this only work for covalent interactions?

THANKS! NOW I CAN UNDERSTAND A PAPER THAT I HAVE TO READ xD

Sir it is in vitro technique????

What is the purpose of using beta actin in this assay sir?

Helpful 👌

r u from Presidency? very good keep up the good work bro..👍

you save me!

great explanation

Amazing explanation, however, isn't this an in-vitro technique? Literally everything is happening outside of the body, in a test tube etc. Thanks, nonetheless.

so by this way you describe yo identify the complex AB not their interaction as say !!!

Who teaches better? A. Your professor majored in biotechnology with 10+ years teaching experience Or B. A random indian boi on youtube

what is this accent ?

good presetation, except some accent, but it's good. thanks.

QuickQuestion You are studying 3 proteins (A, B and C). You hypothesize that A binds to B (forming a complex AB) but not C. From the scientific literature you know that B does not interact with C. 1) You are able to obtain 100% pure preparations of proteins A, B and C. Which experimental technique would you use to prove/disprove your hypothesis? Describe the experiment and the expected results