Antibodies, also referred to as immunoglobulins, are glycoproteins naturally produced in response to invading foreign particles (antigens) such as microorganisms and viruses. As such, they play a critical role in the immune system’s defense against infection and disease.

Antigens recognized and bound by antibodies can be proteins such as receptors expressed on cancer cells, sugars on bacterial and viral cell surfaces, hormones, chemical compounds, or nucleic acid structures. The region of an antigen that interacts with an antibody is called the epitope. Submit here.

Recombinant Antibody Technology

Advances in the understanding of antibody structure and function, bacteriophage replication, and DNA manipulation and mutagenesis led to the development of a method for the generation of recombinant monoclonal antibodies using phage display antibody libraries. 

This technology addresses the limitations of the traditional hybridoma method, which is known to be time consuming and expensive, requiring extensive expertise, as well as specialized cell culture and animal facilities. https://bit.ly/3b6DTkt

The classical representation of an antibody is as a Y-shaped molecule composed of four polypeptide subunits with two identical heavy and light chains (Figure 1). The N-terminus of each heavy chain associates with one of the light chains to create two antigen-binding domains. These are the arms of the “Y” shape and are termed fragment antigen binding (Fab) domains.