Human LR3 IGF1 - P4431X

Human LR3IGF-I is more potent than IGF-I in vitro and in vivo. This increased potency is due to reduced binding of LR3IGF-I to most of the IGF binding proteins which modify the biological actions of IGF-I. Human LR3IGF-I binds to the type 1 IGF receptor with similar affinity to wild type IGF-I.

LR3IGF-I was developed by NovoHelix specifically for supplementation of mammalian cell culture to support the survival and proliferation of cells. It is engineered to have a higher biological potency than native IGF-I or IGF-II and has several advantages over recombinant insulin. Supplementation of cell cultures with LR3IGF-I at a much lower concentration results in equivalent or better productivity than supplementation with standard concentrations of insulin. LR3IGF-I is better able to stimulate the type I IGF receptor and thus induce a higher level of activation of intracellular signaling molecules which are responsible for promoting cell survival by inhibition of apoptosis.