FasL mono, di-, and trimers
John_Richburg at mail.utexas.edu
Tue Jan 6 14:23:22 EST 1998
I am doing Western analysis of FasL, specifically for the soluble form
using an antibody that recognizes the proposed cleaved and released
portion of the FasL protein. I homogenized the tissue in buffer that
contains 1 %NP40, 0.5% sodium deoxycholate, and 0.1% SDS plus PMSF,
aprotinin and sodium orthovanadate.
My question is, could dimers or trimers of this protein exist under these
detergent conditions? I seem to see several high mw bands but am having a
hard time justifying them. I even see these band in the positive control
sample of purified soluble FasL protein.
Has anyone had a similar experience? Can noncovalently bonded proteins
remain together under the conditions above?
Thanks in advance,
College of Pharmacy
Division of Pharmacology and Toxicology
The University of Texas at Austin
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