recombinant proteins – Page 2 – BioProcessing Journal

Kinetic of Expression Study of the Hepatitis B Surface Antigen in Pichia pastoris

In general, yeasts offer advantages for recombinant protein expression because their intracellular environment is suitable for the correct folding of recombinant proteins and grow very high cell densities in defined fermentation media. Within the yeast kingdom, Pichia pastoris has been successfully used for expressing several recombinant proteins. The genome of this yeast contains two copies of the alcohol oxidase (AOX) gene, where the AOX1 promoter regulates 85% of the alcohol oxidase activity and drives the recombinant protein expression into the cell. One of the most successfully recombinant proteins expressed in Pichia pastoris is the hepatitis B surface antigen (HBsAg). The current manufacturing process of the active pharmaceutical ingredient (HBsAg) of the Cuban hepatitis B vaccine (HeberBiovac™ HB) starts with the expression of the HBsAg in Pichia pastoris….

Biologics Production

antigen expression fermentation hepatitis B surface antigen kinetic of expression process optimization protein expression recombinant proteins

Cell Culture Bioreactor Optimization: Growing Recombinant HEK293 Cells to Produce a G-Protein-Coupled Receptor (rGPCR) Membrane Protein

Heterologous expression of membrane proteins remains a bottleneck for structural characterization by x-ray crystallography. Such proteins represent approximately 30% of the proteome and are not sufficiently represented in the Protein Data Bank (PDB). G-protein-coupled receptors (GPCRs) are an area of particular interest as it is estimated that one third of current FDA approved drugs act through this class of receptors. We have been studying rhodopsin with an interest in determining the conformational change that leads to signal transduction in this class of receptors. Although there has been some success in expressing select members of the large GPCR family in bacterial systems, the best characterized expression systems have generally been in mammalian tissue culture…

Biologics Production

cell culture bioreactor G-protein-coupled receptors membrane proteins protein expression recombinant proteins stirred-tank bioreactor

Development and Validation of a Calcium Mobilization Assay for the Detection of Neutralizing Antibodies to Alefacept in Human Serum

The recombinant protein alefacept (Amevive®) is an immunomodulator approved for the treatment of moderate to severe chronic plaque psoriasis. In phase 3 clinical studies, treatment of psoriatic patients with alefacept at a safe and well-tolerated dose caused meaningful reductions in psoriasis area and severity index and in physician global assessment scores as well…

Biologics Production

alefacept anti-drug antibodies anti-psoriatic therapeutics calcium mobilization assay immunogenicity recombinant proteins

Rapid Development of High-Performance Stable Mammalian Cell Lines for Improved Clinical Development

Since the first approval for human use of a recombinant protein therapeutic, this sector of the pharmaceutical market has grown rapidly. The first approved protein therapeutics were small, non-glycosylated proteins such as insulin and human growth hormone; they were produced in bacterial systems. With the advent of mammalian cell-based production systems, it became possible to produce more complex, glycosylated proteins for use as recombinant therapeutics…

Biologics Production

cell line selection mammalian cell line development recombinant proteins stability therapeutic proteins vector construction

Transient HEK293 Recombinant Protein Production Flow: The Replenishment of Protein Batches By Outsourcing to a Contract Research Organization

In order to unravel new protein activities and functions, we have expressed and purified a large number of human proteins. We have chosen to study secreted proteins and the extra-cellular domains of putative single transmembrane domain-containing proteins. In order to retain the natural protein characteristics as far as possible, we have used a mammalian expression system. Human embryonic kidney (HEK293) cells were chosen as they have been shown to possess a high protein-secretory potential. The secreted proteins were expressed with a carboxy-terminal tag and purified by affinity chromatography. Each protein was produced at a routine scale from 500 ml cell cultures, and the secreted protein was purified from the culture supernatant…

Biologics Production Research

contract research outsourcing protein expression protein production pipeline purification recombinant proteins

Enhanced CHO Cell Performance With a Combination of CellPrime™ Recombinant Transferrin and LONGR³IGF-1

With the continued growth of the biopharmaceutical market, the cell culture industry has seen a major shift away from the use of serum and other animal-derived supplements in the manufacture of biopharmaceuticals. Indeed, supporting guidance from the EMEA and FDA for the manufacture of biopharmaceuticals and medical devices encourages the use of “animal-free” components. The key driver for this can be attributed to the increased concern with contamination from adventitious agents such as transmissible encephalopathies…

Biologics Production

cell culture growth factor recombinant proteins recombinant transferrin serum-free media

Product Characterization of Recombinant Proteins and Monoclonal Antibodies

The analytical characterization of recombinant protein therapeutic drug products has broadened to include the use of more sophisticated technologies. The expansion of technical abilities has translated into increasing the depth and breadth of our knowledge and understanding of the drug product intended for commercialization. With the availability of more precise methods, the regulatory expectations for understanding the characteristics of a protein therapeutic drug product are increasing. A thorough understanding of a therapeutic protein’s biochemical and biophysical characteristics is necessary to support investigational new drug (IND) applications and other drug regulatory filings…

Regulatory

analysis characterization monoclonal antibody recombinant proteins standards therapeutic proteins

Effects of Tobacco Extract and Temperature On the Stability of the Monoclonal Antibody CB.Hep-1 Expressed in Transgenic Tobacco Plants

Proteins are widely used in research, medicine and industry, but its extraction from their natural sources can be difficult, tedious and expensive. Therefore, a simple and inexpensive system that allows large-scale production of safe recombinant proteins will always be highly desirable. Traditional production systems that use microbial, insect and mammalian cell cultures have drawbacks, in terms of cost, scalability and product safety. Several studies have shown that molecular farming in plants has many practical, economic, and safety advantages as compared to these conventional methods. Thus, the use of plants for recombinant protein synthesis is gaining wide acceptance…

Biologics Production

molecular farming monoclonal antibody plantibody proteolytic degradation recombinant proteins stability transgenic plants

The Potential for the Use of Baculovirus Expression Vector Systems to Produce Recombinant Protein for Clinical Use

The biologics market, although difficult to estimate, is currently thought to be in excess of $20 billion. In recent years, the growth in the novel therapeutics market has continued to exceed all but the most optimistic of expectations. The number of products in early stage trials may already be over 1,000, with an estimated 40 or so additional products in the process of finally being released to the market. The biologics market is led by relatively few “blockbuster” drugs, but the breadth of novel products continues to expand. This has resulted in exciting times for clinicians but has resulted in concern related to the bottleneck of production capacities for these drugs, as well as the pressure from healthcare agencies to reduce the cost of goods…

Baculovirus Expression Technology Biologics Production

BEVS cost reduction insect cell technology rapid response recombinant proteins vaccines

Glycosylation Design in Transgenic Moss for Better Product Efficacy

Biopharmaceuticals are predicted to become the main driving force of the pharmaceutical market in the near future. Other than blockbuster products such as erythropoietin, an increasing number of approved recombinant therapeutic proteins are based on antibody technology (e.g., fusion proteins or monoclonal antibodies [MAbs]). In contrast to relatively simple products produced in Escherichia coli bacteria (e.g., insulin), proteins which require complex posttranslational modifications such as glycosylation have to be produced in eukaryotic cells. In this context, production systems have been dominated by mammalian cell culture. Nevertheless, alternative eukaryotic expression technologies based on yeast, insect cells, transgenic animals, or transgenic plants are under development. Plants are a particularly promising alternative to mammalian cell culture because of their excellent safety aspects and estimated cost-efficient upstream/cultivation processes. In addition, plants are well known for their ability to express biologically functional monoclonal antibodies. In comparison to the seed plants most widely used for transgenic protein expression — tobacco, corn, and rice — mosses provide unique, beneficial features…

Biologics Production

antibody expression eukaryotic expression glycosylation plant-based protein production recombinant proteins transgenic plants

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