For the next time, you should run 2 gels to resolve both pERK and ERK at same time. For stripping and re-probe, it is better to try a less stringent stripping buffer.

It is probably a good idea to run two seperate blots, because stripping might also decrease the protein bound to the membrane you are using (unless its PVDF). Is it PVDF or nitrocellulose? In any case, 10% SDS seems like a harsh treatment? 

You can run two gels and normalize them to a third protein like tubulin, although I would chose one that is not too abundant, remember you don't want a saturated signal. OR you can use a total ERK antibody of another species, rabbit anti-pERK and mouse anti-total ERK. A wash with 1% azide will kill the activity of the HRP from your first secondary antibody, so you can reprobe without stripping. Using dylight conjugate antibodies (in red and green) will allow you to overlay your images (= yellow). See Licor for more info on this. The advantage is also that the signal does not saturate, so you get better quantification (versus ECL)

Hi Marta, I analysed pAKT and AKT, and I used the classical strong stripping  and mild biorad stripping without any problems, I think  SDS 10% is too much.

Strong: 2% SDS , 62,5 mM Tris HCl pH6,8 ,100mM b-mercaptoethanol, 30 min at 50°C, Mild: 0,1M Glycine 20 mM Magnesium acetate (4H2O), 50 mM KCl, pH 2,2. If you want to try and you need more details I will send you the protocols.

In general I used to incubate on the same membrane, so I try to use an antibody for normalization without a strong signal, for example GAPDH, or at different molecular weight so I can cut the membrane. If you do not have GAPDH or you prefer to incubate tubulin, try to diluite your primary and secondary antibody to avoid a saturated signal as Jonathan said.

Thank you so much for your answers.