An efficient method for native protein purification in the selected range from prostate cancer tissue digests.

ABSTRACT:

Background

Prostate cancer (CP) cells differ from their normal counterpart in gene expression. Genes encoding secreted or extracellular proteins with increased expression in CP may serve as potential biomarkers. For their detection and quantification, assays based on monoclonal antibodies are best suited for development in the clinical setting. One approach to obtain antibodies is to use recombinant proteins as immunogen. However, the synthesis of recombinant protein for each identified candidate is time-consuming and expensive. It is also not practical to generate high quality antibodies to all identified candidates individually. Furthermore, non-native forms (e.g., recombinant) of proteins may not always lead to useful antibodies. Our approach was to purify a subset of proteins f

SUBMITTER: Ahmad R 

PROVIDER: S-EPMC5627993 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature