Protein characterization, purification, and sequence analysis data for plant-made catfish interleukin 22

Abstract

Production and purification of a novel protein in plants results in the generation of multiple data sets leading to an optimized protocol for recovering the recombinant protein. This article presents the data collected in the process used to produce, purify and validate a catfish interleukin 22 (cfIL-22) expressed using a plant-based platform. A commonly used workflow for confirming optimal expression and extraction of the recombinant protein was employed and is outlined herein. The complete research article, including activity analysis of plant-produced cfIL-22, is published in Journal of Biotechnology Elkins and Dolan [1]. Data collected in optimizing the expression, purification and characterization process of cfIL-22 includes stained protein gels and western immunoblot analyses, DNA and protein sequencing, post-translational modification predictions and protein structure predictions. The value of this data lies not only in future work in expressing interleukin 22 orthologs but also provides a guide for optimizing the production and validating similar complex animal/human proteins produced in plants.