Proteomics: recombinant protein production, purification and characterization

The usability of recombinant proteins across diverse applications largely depends on their similarity to physiological counterparts. To maximize the probability of achieving a successful protein it is necessary to conduct proteomic studies for its deep characterization. These studies, among other objectives, aim to identify the purified protein, ascertain its molecular weight, and analyze post-translational modifications or putative molecular interactions.

Description

Proteomic studies using mass spectrometry play a crucial role in establishing production and purification procedures for recombinant proteins on a case-by-case basis and ensuring their quality for various applications. They provide valuable information on the identity, purity, structural integrity, consistency, reproducibility, and functional aspects of these proteins, ultimately contributing to the success of various biotechnological and biomedical applications.

Examples of CIBER BBN collaborative intramural  projects implementing this Cutting-Edge Biomedical Solution:

Recently, two collaborations have been conducted, enabling the supply of properly identified active recombinant proteins to the client.

• In one of the projects, successful purification of an active recombinant protein from Stenotrophomonas maltophilia was achieved using the E. coli expression system. Purification of this protein had not been accomplished until now. These results are pending publication. 

• In the second project, a human enzyme has been purified using the E. coli expression system for industrial purposes. It is pending of commercialization.

Both proteins were designed, produced and purified by U1, and finally characterized by U30. To preserve the confidential rights of our users, we cannot provide more details on the type of protein nor the name of the companies.

More info: https://www.nanbiosis.es/proteomics/