Hi! I have a question... I'm doing densitometric analysis of native and sds under non reducing conditions. I'm trying to figure out the nature and ideally a percentage of the type of my protein aggregates (i.e. covalent or non covalent), so I'm thinking... If I substract the band intensity of SDS-NR - native band intensity of the same protein, is it reasonable to say that that difference is my protein that's involved in non covalent assoaication? Thank you so much!!❤️
I love that you show the actual lab setting. Gives me a better frame of reference.
Glad you find it helpful!
This is the best explanatory vide I've ever seen!!!!!!!!!! THANK YOU SO MUCH!!!!
So glad it was helpful!
Hi! I have a question... I'm doing densitometric analysis of native and sds under non reducing conditions. I'm trying to figure out the nature and ideally a percentage of the type of my protein aggregates (i.e. covalent or non covalent), so I'm thinking... If I substract the band intensity of SDS-NR - native band intensity of the same protein, is it reasonable to say that that difference is my protein that's involved in non covalent assoaication?
Thank you so much!!❤️
Hi - I'd be worried that the different conditions might influence the staining
@@thebumblingbiochemist
oh ok great point!
Thank you so much 😊
Great post. This is just what I need.
Happy I could help!
Awesome channel! Thank you so much.
Thanks so much!
OMG you're AWESOME!!!! What a lifesaver :D
Thank you! So glad it was helpful
thanks for sharing!this helps me a lot
Glad it helped!
Thank you. Reallh helpful.
Glad it was helpful!
Have you tried native PAGE with proteins statically bound to nucleic acids?
as in an EMSA? I have content on that
@@thebumblingbiochemist Yeah, EMSA's close.