News/Events

From all of us at Proteos, we wish you a joyful holiday season and a healthy, prosperous New Year.

From all of us at Proteos, Happy Thanksgiving!

Get Ahead of Your Year-End Research Goals!

The production of recombinant proteins, particularly antigens, involves several critical variables.

Conducting small-scale pilot experiments is key to identifying the optimal expression conditions for recombinant proteins.

Generating multiple protein constructs through alteration of affinity tag selection, size, and placement can be highly beneficial for projects with no prior precedent of successful recombinant protein production.

At Proteos, we are committed to delivering high-quality services that surpass client expectations. This begins with selecting the optimal expression system and designing a scope of work that is appropriate for your protein of interest.

Producing novel recombinant proteins can be a complex endeavor, but understanding the key variables involved can make a significant difference. Beginning with a pilot experiment is a strategic move.

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.