One way would be to use a centrifugal ultrafiltration device, such as a Microcon.

https://www.emdmillipore.com/US/en/product/Microcon-Centrifugal-Filters,MM_NF-C113861?ReferrerURL=https%3A%2F%2Fwww.google.com%2F

A less expensive way would be to precipitate the protein using trichloroacetic acid (TCA). In 1.5-ml microcentrifuge tubes, add 1/10 volume of 72% (w/v) TCA to each sample. Incubate on ice for 10 minutes. Centrifuge at the maximum speed of the microcentrifuge for 10 minutes. Carefully remove the entire supernatant without disturbing the precipitate. Dissolve the precipitate in SDS-PAGE sample buffer.

I prefer lyophilization. However, precipitation is the most straightforward method, using five volumes of 95% acetone.

Hi,

TCA precipitation would be a good option for you.

Hi,

There are alternative approaches available for conducting western blot experiments. If your research primarily targets highly abundant proteins, you may opt for organic precipitation methods like Methanol: Chloroform, TCA, or Acetone precipitations. At same time, it's important to consider several factors, such as the specificity of your protein of interest (which may require immunoprecipitation), as well as the stability of the protein throughout the precipitation process. So, the choice of method should align with your specific experimental requirements.

Thanks for your valuable suggestions and the protocol worked very well. Venkatakrishna LM Thanks again@@@