Yes, depending on the concentration of SDS. The SDS might denature your protein of interest. The antibody in your ELISA might not recognize the epitope. You can use a 1% NP40 buffer (in a tris or HEPES buffer supplemented with 150mM NaCL and protease inhibitors). You will also need an efficient way of grinding the tissue piece using a homogenizer.    

I agree with Richard.  Using 1-2% NP40 buffer is a good option because it is a mild detergent.  You want to avoid using a stringent detergent if you are using the same tissue homogenate for elisas.  You could also homogenize the tissue in detergent free buffer.  We use a homogenization buffer that contains 10 mM tris, 1 mM EDTA, and 200 mM sucrose when we are performing IPs from tissue where the protein cannot be denatured by detergent.  Do you have enough tissue to process half with detergent for the western and half with detergent free for the elisa?  Good luck 

Thank you both for your answers. I have been leaning towards using a detergent-free protocol (actually, the ELISA manufacturer recommends homogenising in PBS with 3 freeze-thaw cycles). Richard - I will be using a Qiagen TissueLyser, which I'm led to believe gives good yields suitable for WB. Brandon - to answer your question, yes I do have sufficient sample to perform two separate homogenisation protocols, and had wondered whether the best thing to do would be to homogenise separately for WB and ELISA. In my situation, is this what you would do?

Thanks again to you both

Depends on what you're blotting and detecting by ELISA. If it's cytosolic proteins, do a hypotonic lysis without detergent and its a one step homogenisation.

If it's membrane proteins, use a non-detergent extraction technique, where you replace detergent with something like NDSB (Calbiochem). 

Alternatively, use CHAPs detergent 0.3 %(w/v), it will solubilise membranes and we use it for assaying enzymes from mouse and human tissue, which I think is compatible with ELISA protocols too.