Hello,

We had been trying to identify a drug target in MRSA by running biotin pull down assay. Our lysate buffer is composed of 10 mM Tris HCL, 20 mM EDTA, sucrose and 20mg/ ml lysozyme and we further sonicate the bacterial pellet in order to release the proteins. We did not use any protease inhibitor during the assay. For both the wash and the biotin- streptavidin treated sample, we obtained only one single band. Is it that our proteins are getting degraded due to the lack of protease inhibitor? Is there any protocol specific for isolating proteins in MRSA?