Main > PROTEINS > Purification > Org.: CA. USA. DM (ELP/Patent) > Report Abstract

Large-scale protein purification usually requires a chromatographic separation, which can be expensive and time-consuming. Two independent groups now describe a fast, inexpensive way to purify recombinant proteins using tags called elastin-like polypeptides (ELPs), which are attached to the protein through a self-cleaving linker. When these ELP tags are heated above a transition temperature in the presence of salt, they precipitate, taking the fusion protein with them. Following the separation, the conditions are adjusted so that the linker cleaves itself, liberating the purified protein. The researchers, use microfiltration to separate the precipitated proteins from the rest of the mixture


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