News/Events

Our third and final blog post discussing fusion proteins for prokaryotic expression will cover placement and removal of the fusion protein.

Selection of a suitable fusion partner to enhance soluble expression and serve as an affinity tag for recombinant protein production in prokaryotic expression systems (E. coli) is a crucial step that should not be overlooked during construct design.

Fusion proteins are used to improve the solubility of recombinant proteins produced in prokaryotic cells.

There are several reasons why a recombinant protein may not be properly secreted.

Proteos is dedicated to sharing our good fortune with the community.

Proteos would like to wish you a very Happy Thanksgiving!

Selection of the proper signal sequence for recombinant protein production in mammalian and insect cell culture is a crucial step that should not be overlooked during construct design.

It’s with immense pride and gratitude that we celebrate 20 years of delivering excellence in recombinant protein production for the life science community.

Proteos recently upgraded its eukaryotic expression capabilities with the purchase of 4 high-capacity reach-in incubator/shaker systems built by Eberbach Corporation, Belleville, Michigan.

Workflows for tackling challenging protein projects often utilize an affinity tag approach. In previous posts, we have discussed the purpose of utilizing affinity tags in recombinant protein production, the importance of selecting the proper tag for your specific protein target, and the importance of tag placement that can influence protein expression, purification, and functionality. Our final post in this series will discuss removal of affinity tags.

A eukaryotic signal sequence is a series of amino acids that targets a protein to the secretory pathway.

As Memorial Day approaches, Proteos would like to extend our warmest wishes to you and your loved ones for a safe and enjoyable weekend.