I haven't tried, but most likely yes; binding of His-tagged proteins to IMAC resins is pretty munch insensitive to most reagents, except those that compete with binding (e.g. histidine or imidazole), chelating reagents like EDTA, which will strip the metal off the resin, or low pH, which will protonate the imidazole side chain of His residues. Beware that the detergent in the lysis buffer may denature fragile proteins; however, you should be able to get rid of it by washing the resin extensively with detergent-free buffer before eluting.

I agree with Pierre on the details. I believe Pierce's Y-Per, B-Per, etc are compatible with His-tagged purifications, and they report that the detergent does not denature proteins. I haven't used Y-Per extensively, but I recall we got the best yields vortexing with glass beads after resuspending in Y-Per.