Recombinant antibodies are created through a process of genetic engineering, where the genes that encode for the antibody’s variable regions are isolated and inserted into a vector. The vector is then used to transform cells, which will produce the recombinant antibody.
Recombinant antibody production can be used to create monoclonal or polyclonal antibodies. Monoclonal antibodies are created from a single clone of cells, meaning they all have the same antigen-binding site. This makes them ideal for specific applications, such as targeting a particular disease.
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Polyclonal antibodies are created from multiple clones of cells and will therefore have several different antigen-binding sites. This makes them more versatile, but less specific than monoclonal antibodies.
Recombinant antibodies have a wide range of applications, including in diagnostics, therapeutics and research. There are a number of different protocols that can be used to produce recombinant antibodies. The most common is the hybridoma technique, which involves fusing antibody-producing B cells with cancerous myeloma cells. Other methods include phage display and transgenic animals.
The advantage of using recombinant antibodies is that they can be created in large quantities and with high purity. They can also be tailored to specific needs, such as by changing the amino acid sequence of the variable region.