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Updated: Nov 5, 2025

Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach
Published on: October 16, 2014
Recombinant Protein Production and Purification Using Eukaryotic Cell Factories
1Paris-Saclay University, Orsay, France. amissoum93@gmail.com.
Abstract:
Cloning proteins enables their production and characterization for further studies. This requires inserting the gene of the studied protein to be inserted in a vector, which then will be transformed to the host cell used as "factory." Consequently, the "biomass" of host cells will be produced using bioreactors. Here we describe the production of Rhizomucor miehei lipase (RML) by cloning the corresponding genes in the yeast Pichia pastoris. This enzyme is used as a biocatalyst for biofuel production. The successfully produced recombinant proteins are then purified using ion exchange chromatography.

