Growth factors can be synthesised in prokaryotic cells, most commonly E. coli, or eukaryotic cells, using cell lines such as human embryonic kidney (HEK) 293 cells or Chinese hamster ovary (CHO) cells. There are benefits to each of these cell sources. Proteins produced from prokaryotic sources generally have less lot-to-lot variability and higher purity than eukaryotic systems. They have the additional benefit of being animal-free, eliminating the risks of contaminating growth factors, viruses, prions and other animal-derived ingredients.  This production method also reduces the need for foetal bovine serum (FBS), use of which is an ethical concern for many researchers. However, when it comes to complex full length mammalian proteins prokaryotic systems can fall short; protein refolding and post translational modification can differ from eukaryotic systems which can affect protein solubility and activity. For growth factors from both prokaryotic and eukaryotic sources, please be sure to check the bioactivity data before you purchase.

Innovations in growth factor production are allowing an increasing number of proteins to be produced using prokaryotic systems, and they benefit from being animal-free, while maintaining correct refolding and activity. Qkine is leading this charge with products including; TGF-β1 PLUS, the first entirely animal-free TGF-β1, and bioactive fragments of human R-spondin 1 and R-spondin 3.