Can someone help me with the following problem? I am trying to run a western blot against
surface protein on a native gel. The protein is not reactive with the antibody in a reduce form,
thus the native gel. The problem is the surface protein will not migrate into the gel in its native
form. I stain the gel with Coomassie Blue and clearly see the protein getting stuck in the 4%
stacker. My sample buffer contains 3.125% SDS in a 0.1 M Tris buffer. Does anyone know of a
protocol that would allow me to keep my protein in its native form on an SDS-PAGE gel? Thanks
in advance for any information.
