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Therapeutic proteins (Biologics/Biotherapeutics) are active biomolecules are derived from a biological source by production in microorganisms or cells (humans and animals) using biotechnology.

Protein therapeutics exhibit complex secondary and tertiary structures that must be maintained to exhibit the desired function. Protein therapeutics cannot be completely synthesized by chemical processes and have to be manufactured in living cells or organisms; consequently, the choices of the cell line, species origin, and culture conditions all affect the final product characteristics. Moreover, most biologically active proteins require posttranslational modifications that can be compromised when heterologous expression systems are used. Additionally, as the products are synthesized by cells or organisms, complex purification processes are involved. Furthermore, viral clearance processes such as removal of virus particles with filters or resins, as well as inactivation steps by changing pH or detergents, are implemented to prevent the serious safety issue of viral contamination of protein drug substances.

So far, more than 100 proteins have been approved by FDA as registered therapeutics. Many others are undergoing clinical trials. These approved recombinant proteins include biotechnology medicines, antibody-drug conjugates, vaccines, enzymes, natural/recombinant cytokines, and interferons.

Proteins are proven effective even as vaccines that help stimulate the body’s natural defense mechanism for immunogenic response. By the help of cloning and expressing cDNA that encodes heterologous proteins, these therapeutic proteins have gain attractions in the pharmaceutical industry.

In the past, the major method to obtain a specific protein was isolation from a natural source, generally inefficient and time-consuming. Over decades, the source and methodology for the production and purification have gone through major developments. Recombinant DNA technology is now widely used for production of many recombinant therapeutic proteins, for instance using mammalian Chinese hamster ovary cells (CHO). Therapeutic proteins, with the advance of recombinant DNA technology, are now produced industrially in bacterial, yeast, or mammalian expression systems.

Escherichia coli (E.coli), as a microbial host, has long been employed for production of different types of proteins. S. cerevisiae and P. pastoris are also known to be efficient microbial hosts for better expression and production of therapeutic proteins. In addition, cell-free in vitro systems are now developed, which allows a one-pot reaction for transcription and translation of DNA fragments. Animal cell cultures have also been widely used for the production of various human therapeutic proteins. Unlike the microbial production system, animal cell cultures can carry out posttranslational modifications and present more reliable biological activity. Alternatively, transgenic animals are gaining more attention for production of therapeutic proteins. Besides, many transgenic plants have also been used for the production of different types of therapeutic proteins.

After production, therapeutic proteins need to be purified from proteinaceous and nonproteinaceous components. Several methodologies have been adopted for the purification of therapeutic proteins including chromatography, precipitation, differential solubilization, extraction, and ultracentrifugation.

Creative BioMart provides high quality and purity therapeutic proteins in both recombinant and native forms, which are specific for research use and industrial raw materials. Please contact us for more products information.

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