I'm new to mass spec/proteomics and hoping for some advice! 

We want to do mass-spec on the pulldown from an immunoprecipitation.  We are concerned about IgG/antibody contamination in the sample.

Unfortunately, chemically crosslinking (with DSS) our antibody to the beads decreases the activity of our antibody. Silver staining of our IP product shows that we lose a significant amount of target proteins with antibody crosslinking,although it does eliminate IgG elution.

We are looking for a way to reduce IgG elution, without having to crosslink.  Due to budget constraints, we would also like to avoid alternative (expensive) antibody coupling techniques (such as the surface activated Epoxy m270 dynabeads).

I've found some papers suggesting "soft elution"  (https://www.ncbi.nlm.nih.gov/pubmed/21448433) to reduce IgG contamination. Does anyone have experience with this?

Alternatively, is it possible to simply excise the IgG heavy and light chain bands from the gel, and submit the rest of the lane for mass spec?  

Thanks for any help!