i made an error in my description of the gel we used to separate the myosin isoforms (forgive me, we published in 1983 and i haven't used it since).
the gel was 3.2-5% acrylamide with a 0-8M urea gradient. the stack was 2.8%.
i will pm you with the paper and two supporting papers.
western blot
Started by distazio, May 27 2009 02:54 AM
17 replies to this topic
#16
Posted 05 June 2009 - 10:31 AM
talent does what it can
genius does what it must
i do what i get paid to do
genius does what it must
i do what i get paid to do
#17
Posted 07 June 2009 - 06:59 AM
thanks you are really nice! i'll ready the papers. thank u.
i have another question: is it possible to obtain a specific protein cleavage?? and how??
mt
i have another question: is it possible to obtain a specific protein cleavage?? and how??
mt
#18
Posted 08 June 2009 - 08:13 AM
you can get a sort of specific cleavage. proteases will cleave at specific residues. but, you usually find several cleavage sites on your proteins.
in some cases you can introduce a specific site that is unique to a specific protease (eg thrombin) and is not otherwise found in your protein.
in some cases you can introduce a specific site that is unique to a specific protease (eg thrombin) and is not otherwise found in your protein.
talent does what it can
genius does what it must
i do what i get paid to do
genius does what it must
i do what i get paid to do














