Posted 28 June 2010 - 10:18 AM
I am writing to know your opinion about some strange results I got while performing WB.
#1. Is that possible that different antibodies for the same protein stain at different molecular weights? If yes, why does that happen?
#2. I used RIPA buffer (+ protease inhibitors) to extract samples from mouse tissue. I incubated the membranes (NC) with the ab ON (4C) in 1% milk solution in TBST and, with one of the antibodies I got good results but when I tryed to replicate them in the same conditions I got a lot of extra bands and the more intense band is lower than the correct protein molecular weight. I have no idea about what might be happening and how I can get rid of the extra bands.
All help/ ideas are welcomed.
Posted 28 June 2010 - 12:54 PM
Posted 28 June 2010 - 03:08 PM
Posted 28 June 2010 - 07:56 PM
Sometimes the antibodies are not as good as they say in the datasheet!
"This is SPARTA!"
"I´m the goddamn batman"