Related Experiment Video
Updated: Jun 30, 2026
Isolation and Genetic Manipulation of Adult Cardiac Myocytes for Confocal Imaging
Published on: September 17, 2009
Purification and molecular characterization of recombinant rat betacellulin
A J Dunbar1, I K Priebe, M P Sanderson
1Cooperative Research Centre for Tissue Growth and Repair, CSIRO Health Sciences and Nutrition, PO Box 10065 Adelaide BC, South Australia 5000, Australia. andrew.dunbar@gropep.com.au
Abstract:
A method for the large scale expression and purification of rat betacellulin (BTC) from Escherichia coli has been developed using a cleavable fusion protein strategy. Insoluble fusion protein collected as inclusion bodies was dissolved in urea under reducing conditions, re-folded, and purified by gel filtration chromatography and C(4) RP-HPLC. Authentic rat BTC was obtained after proteolytic cleavage of the fusion protein with Factor Xa. Factor Xa cleaved an additional site within the BTC protein, generating a truncated isoform separable from full-length BTC by heparin-affinity chromatography. Recombinant rat BTC stimulated the proliferation of mouse Balb/c 3T3 fibroblasts and competed for binding to the ErbB1 receptor in a dose-dependent manner analogous to that of BTC purified from natural sources.
