FasL mono, di-, and trimers

[John Richburg]

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,

john

-- 
John Richburg
Assistant Professor
College of Pharmacy
Division of Pharmacology and Toxicology
The University of Texas at Austin
512-471-4736