Now that you have provided some details, it helps a little. It seems that you are trying to recover protein fraction after RNA extraction and in it there is a protein (or many proteins) that you like to quantitate by ELISA; correct?

The term "protein coating" is normally used in relation to the antibody used to capture an antigen in ELISA, and in reference to a non-specific protein (or protein mixture) used to saturate the binding capacity of the plastic plates. If all goes well, the rest of all of the interactions in an ELISA are quite specific (antigen-antibody binding).

There are some cellular proteins (complexes) that do get irreversibly denatured by phenol chloroform that would be quite difficult to dissolve (not necessarily impossible). However, if you know the nature of your protein, it may help to determine how you should proceed.

As for loading the dissolved protein in 1% SDS directly into the plate and expecting it to bind to the capture antibody, it will not happen. If you know enough about your capture antibody, you may have an option where you could sufficiently dilute SDS into a buffer where the concentration drops to ~0.05% or less, you may succeed, provided your protein remains soluble and the antigenic epitope(s) are recognized by your capture antibody. Of course, this assumes that the protein of your interest is sufficiently abundant that even after 20-fold or higher dilution, it will remain in the reliable range of your standard curve. If you have reasons to believe that it may work, remember to add equal amount of SDS to your standards as well.

Highly unlikely* to impossible!

* unlikely is included only because at a very low frequency, just about anything may be possible.  ;)

I think I have used a "detergent removal column" once from Pierce that worked quite fine (simply size exclusion I guess) - maybe check their homepage to find if it's also useful for purifying the proteins your coating experiments.

Tausif is right. Very highly unlikely to work. I would not recommend trying it.

I don't think protein dissolved in 1% SDS can stick to elisa plates. Best option is to either dialyze using dialyzing cassette to get rid of SDS or use column (as Christian mentioned).

you can try to precipitate you proteins with acetone or ethanol from the 1% SDS  and them  dissolve them in sodium bicarbonate buffer 50mM. 

There are numerous ways to remove ionic (and non-ionic) detergents from solutions. However, it depends on the nature of protein if some or any of the procedures will be useful.

Since the question is phrased in a way ("dissolved") which leads me to think that the presence of detergent is obligatory for dissolution process (for example, in cases of tightly membrane-bound proteins), removal of detergent will most likely cause precipitation of protein. If my assumption is incorrect and the protein in question is perfectly soluble in a garden variety aqueous medium, perhaps the question could have been better phrased by stating: my protein solution "contains".... 

thank you all for my query 

I actually using trizol method for RNA as well as protein isolation from same sample which is recommended by Lifetechnology, But my protein is not get fully dissolve in the 1% SDS. and I want to do ELISA for these extracted proteins. Any suggestion what to do? 

Now that you have provided some details, it helps a little. It seems that you are trying to recover protein fraction after RNA extraction and in it there is a protein (or many proteins) that you like to quantitate by ELISA; correct?

The term "protein coating" is normally used in relation to the antibody used to capture an antigen in ELISA, and in reference to a non-specific protein (or protein mixture) used to saturate the binding capacity of the plastic plates. If all goes well, the rest of all of the interactions in an ELISA are quite specific (antigen-antibody binding).

There are some cellular proteins (complexes) that do get irreversibly denatured by phenol chloroform that would be quite difficult to dissolve (not necessarily impossible). However, if you know the nature of your protein, it may help to determine how you should proceed.

As for loading the dissolved protein in 1% SDS directly into the plate and expecting it to bind to the capture antibody, it will not happen. If you know enough about your capture antibody, you may have an option where you could sufficiently dilute SDS into a buffer where the concentration drops to ~0.05% or less, you may succeed, provided your protein remains soluble and the antigenic epitope(s) are recognized by your capture antibody. Of course, this assumes that the protein of your interest is sufficiently abundant that even after 20-fold or higher dilution, it will remain in the reliable range of your standard curve. If you have reasons to believe that it may work, remember to add equal amount of SDS to your standards as well.

You can use provided that 1%SDS storage cant contribute to the conformational changes in the protein structure.

Thanks a lot for information @Tausif Alam

Thanks @ Fazel Gorjipour

How much concentration of Tween20 did you used?

Hi,You can use SDS precipitation kit or dialysis against PBS pH 7.4.

It is preferable that the transferring of protein bands exactly after the running of them to prevent diffusion of proteins specially in non purified proteins. Although, you can keep the gel up to 12 hours at 4◦ C.

Yes, you can

No. You have to remove SDS before coating to ELISA plate. You can remove SDS by dialysis or gel filtration chromatography. SDS generally denatures the protein and thereby there is confrontational change in the antigenic site (epitope). Is your protein comes backs to its original form after removal of denaturing agent from it. Then you have to choose appropriate antibody and labelled antibody for its recognition.