What is a phage or bacteriophage?
Phages are viruses that infect bacterial cells. There are several types of phages that have been used as vehicles for phage display including Ff filamentous phage, Lambda and T7. In phage display, the bacteriophages are used to construct different phage libraries as peptide libraries or antibody library
History of phage display
Phage display technology was first introduced in 1985 by George Smith. After that many advantages have been introduced including the way to construct a phage library like antibody library to select phage display antibodies.
Advantages of phage display
Phage display is a system for large scale study and selection of proteins, peptide and antibodies based on their binding affinity and specificity. One advantage of phage display is the enormous diversity of variant proteins that can be represented in a phage library. Phage display provides a means of rapidly screening large numbers of proteins against potential binding partners.
antibody production

Protein Production

Protein Production

 Today, there are a large number of systems available for protein expression and large-scale recombinant protein production (E. coli, baculovirus-mediated insect cell expression, yeast, and several mammalian based systems). Each has its own respective advantages in relation to cost, ease of use, and post-translational modification.

Escherichia coli-mediated protein expression

Bacterial expression is the most commonly used expression system for the production of recombinant proteins. The organism is relatively simple to manipulate, inexpensive to culture, and the amount of time necessary to generate a recombinant protein is short. However, since it is a prokaryotic based system, heterologously expressed eukaryotic proteins are not modified correctly, and it can also be difficult to facilitate the secretion of large amounts of expressed protein. Furthermore, proteins expressed in large amounts can precipitate, forming inclusion bodies, whilst large complex proteins can also be difficult to propagate.


Baculovirus-mediated insect cell protein expression

Baculovirus-mediated insect cell expression has become one of the most popular vehicles for the productionof large quantities of recombinant protein for structural and functional studies of therapeutically relevant bio-molecules. Baculovirus protein expression is a eukaryotic based expression system and thus provides protein modification and processing patterns similar to those in higher eukaryotic cells. In addition, the baculovirus-mediated system uses a helper-independent virus that can be propagated to very high titres and is easily adapted to suspension culture, making it possible to generate large amounts of recombinant protein with relative ease.

Mammalian cell expression

The expression of heterologous proteins in a mammalian cell expression systems provides several advantages to their production in E. coli or insect cells, including correct post-translational modification and folding. In this system, it is used often the mammalian cells CHO or HEK293. The system utilizes often episomally replicating plasmids featuring the Epstein– Barr virus (EBV) oriP driven by EBNA-1 protein generated from a gene integrated into the HEK293 genome. In most cases, transient protein expression is driven by the strong CMV promoter.

We offer a list of custom protein expression services including gene synthesis, vector construction, pilot expression, process optimization, fermentation and protein purification. Our suppliers has expertise in different expression systems, including cell-free, bacterial, yeast, baculovirus / insect mammalian cell systems. Each protein can be expressed differently in different systems. Each recombinant proten are produced according to our customer specifications or by developing customized protocols in house.

Vrisko Ltd offers a variety of Custom Services to fit your research and production needs including Protein production services. Ask for a quote and additional specific details according to your needs in our “contact us” page.