IBI recombinant proteins are expressed in Pichia pastoris (yeast) system which provides many advantages over E. coli systems. Yeast systems promote proper protein folding and post-translational modifications for greater bio-activity. The recombinant proteins are endotoxin free and are purified without HIS-TAGS or any other TAG. IBI’s yeast expression system has proven to produce more active proteins that more closely resemble their host form.
All IBI recombinant proteins are lyophilized and shipped at room temperature without carrier protein. Proteins can be reconstituted in sterile PBS with at least 0.1% of carrier protein such as BSA or cell assay media.
The IL-8 feline protein can be used in cell culture, as an IL-8 ELISA Standard, and as a Western Blot Control.