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Rather than presenting a whole organism to the immune system, a fragment of the pathogen can be used to trigger specific immune responses. Examples include the subunit vaccine against hepatitis B virus, which is composed of only the surface proteins of the virus.
Subunit vaccines can be composed of a protein or a peptide. While proteins must be produced in a cellular environment, peptides can be synthesized. However, peptides are often only weakly immunogenic. For this reason, a mixture of peptides may be utilized, although whole recombinant proteins are most often used.
Recombinant proteins are typically produced using an expression vector, such as a plasmid. The target gene of interest is cloned into the expression vector and then transfected into host cells. Once inside the cells, the expression vector uses the cell’s machinery for transcription to produce mRNA, and then the translational machinery to produce the protein of interest.
Recombinant proteins are produced in a variety of expression systems including bacteria, yeast, or mammalian cells. After expression of the gene product in cells, the target protein must be purified from the proteins of the host cell. To make the purification process easier, the cloned gene can be labeled with a tag such as histidine.
We offer expression vectors as well as a wide range of products for tagged protein purification.
Since 1982, over one billion doses of hepatitis B vaccine have been used worldwide. This goal has been achieved thanks to the large-scale production of recombinant vaccine. The chromatographic methods used to purify hepatitis B surface antigen (r-HBsAg) are robust and economic. The entire process comprises three chromatographic steps, followed by buffer exchange and product concentration via membrane ﬁltration.
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