Usually NP-40 and triton are considered detergent of comparable potency. So if you wish to replace NP-40 by triton-X-100 and conserve similar conditions, you should use the same final concentration, e.g. 1% NP-40= 1% Triton-X-100. 

Concerning the lysis of your nuclei, I really doubt that either of those detergent will allow you to recover all of nuclei proteins. Usually RIPA is recommended (see Abcam document on the link below for example).

I think that it would be possible to perform a two-step protocol:1) use a non-harsh detergent (such as 1% NP-40) to get rid of cytoplasmic proteins by discarding the supernatant 2) use the RIPA on the pellet-containing nucleus to recover nuclear proteins. Check a bit the literature for what people do to perform their ChIP (chromatin immuno precipitation)

http://wolfson.huji.ac.il/purification/PDF/Immunoprecipitation/ABCAM_ImmunoprecipProtocol.pdf

Hi there,

I don't think there is any problem using Triton, I think however that 1% can be a bit high and you risk dissociation of the complex you try to isolate.

By the way are you not rather thinking about replacing 1%NP40 by 0.1% Triton?... 1%NP40 is usual in CoIP lysis buffer...

You could also look into using tween or digitonin. 

The choice of the buffer detergent is generally based on the kind of proteins being looked into during co-ip. 

If your proteins contain PEST domain in their sequence, I would recommend you to use a Zwitter ion based detergent such as CHAPS. this is expensive, but will surely work in most conditions.

Just to be sure, Do the CO-IP using three or four different buffers and run them on the same gel. This would surely solve all your problems. You use, Triton-X-100, tween-20, NP-40 and others.

Hope this answer has given you some help and insight.

Usually NP-40 and triton are considered detergent of comparable potency. So if you wish to replace NP-40 by triton-X-100 and conserve similar conditions, you should use the same final concentration, e.g. 1% NP-40= 1% Triton-X-100. 

Concerning the lysis of your nuclei, I really doubt that either of those detergent will allow you to recover all of nuclei proteins. Usually RIPA is recommended (see Abcam document on the link below for example).

I think that it would be possible to perform a two-step protocol:1) use a non-harsh detergent (such as 1% NP-40) to get rid of cytoplasmic proteins by discarding the supernatant 2) use the RIPA on the pellet-containing nucleus to recover nuclear proteins. Check a bit the literature for what people do to perform their ChIP (chromatin immuno precipitation)

http://wolfson.huji.ac.il/purification/PDF/Immunoprecipitation/ABCAM_ImmunoprecipProtocol.pdf

I would normally use RIPA buffer to obtain nuclear proteins. Mild detergents such as theTriton and NP-40 ones you mentioned generally will not get you all of the nuclear proteins.

Hi Syed. Use 0.1% tritonX-100 and if that does not work then try using both 0.1%triton and  0.5% Tween20. 

If you are after nuclear proteins use RIPA. Nonidet P-40 and trixton are not very efficient at lysing nuclear membranes.

also watch out for abbreviations, they can be a sucker punch: https://www.researchgate.net/post/What_is_the_difference_between_NP-40_and_Nonidet-P40_for_RIPA_buffer