It is possible, but it depends on your staining method. The classical method using Methanol/acetic acid is more difficult, the colloidal staining methods are not.

See this article on Bitesitebio for more details (it has also another interesting reference): http://bitesizebio.com/9960/second-chance-saloon-how-to-western-blot-a-coomassie-stained-gel/

Another problem is the detection of the proteins afterwards, here you have to use chemiluminescent or fluorescent detection methods. Depositing color precipitates on the membrane will obviously cause problems.

Thanks for the responses. The method outlined in the original article uses isopropanol instead of methanol as part of the staining solution. Maybe that is why it doesn't fix the proteins into the gel, as there is no methanol in the solution. The recipie is 0.25% coomassie blue, 25% isopropanol, 10% acetic acid. Destained with only 10% acetic acid, no methanol. We also have simply blue in the lab, I will try that next time.

I asked this originally because we do western blots on conditioned media, and unlike with cell lysates there aren't any good internal controls to use like actin or lamin etc. So, we've either ran two gels and stained one of them, or used the ponceau stain, which doesn't work very well. We also use serum free media for making conditioned media so we can't use the bovine albumin as a control either.

what about staining a gel after blotting? for quality check, I stain my gel after blotting and detect them (not all of them transferred to membrane, obviously) by CB and get satisfied!

Since it's quite true that Ponceau on PVDF does not really work, I also use to stain the membrane with Coomassie after the WBs, so that you quantify exactly what you are looking at with WB (quantifying what is left on the gel after the transfer might not be always very accurate, it also depends on how much protein you load, below 5 ug per lane there is too little left after transfer...).

The staining protocol is super simple, since the proteins are exposed on the surface of the membrane. Incubation with Coomassie and washes can range between 30 sec and 1-2 min. The washing steps are critical because you have to be sure you wash out all blue from the membrane and obtain a clear pattern of bands over a white background, otherwise you'll have trouble with background subtraction when you want to quantify the total protein per lane.

You can also Silver stain the proteins on the membrane.

In our laboratory, I tried CBB staining for western blot, But, We saw the protein bands very lightly. But, I had standardized the ponceau staining, I got a clear results and very very clear protein bands also seen. My suggestion is ponceau staining for western blot in membrane is very good method.

I have mentioned the staining procedure following:

Transfer of protein and equal loading of protein was confirmed by staining the membrane with ponceau-S dye (0.5 % ponceau-S in 5% glacial acetic acid) and then washed with distilled water.

It is enough for WB stainig.