Introduction to Anti-Epitope Antibody Discovery by Premade Antibody Library

With the deepening of research, antibodies play more and more important roles in the biological field. Functional antibodies, anti-peptide/protein antibodies, anti-epitope antibodies, anti-cell-based target antibodies, and bifunctional antibodies all have their own advantages and characteristics. With different advantages, they play important roles in different fields. Antigenic epitopes are the basic structural units by which antigens bind to antigen recognition receptors (TCRs/BCRs) on the surface of T or B cells and are specifically recognized by antibodies. An antigen may have one or more different antigenic epitopes. And different epitopes may stimulate the body to produce different specific antibodies. Therefore, determining antigenic epitopes during antibody development is critical to the outcome of antibody development. Based on our rich field experience and advanced research platform, Creative Biolabs provides comprehensive services to support premade antibody library screening and anti-epitope antibody discovery.

Anti-Epitope Antibody

Epitopes, also known as antigenic determinants, are small sites on an antigen to which complementary antibodies may specifically bind. These are usually one to six monosaccharides or five to eight amino acid residues on the surface of the antigen. One or more epitopes may be present on an antigenic molecule. Depending on the spatial distribution of epitopes, they can be categorized as conformational and linear epitopes. Since antigenic molecules exist in space, the epitope recognized by an antibody may depend on the presence of a specific three-dimensional antigenic conformation (e.g., a unique site formed by the interaction of two natural protein loops or subunits), which is known as a conformational epitope. Epitopes may also correspond to simple linear sequences of amino acids, which are called linear epitopes.

The range of possible binding sites on the target molecule, also known as the antigen, is enormous, and each potential binding site has its own structural properties derived from covalent, ionic, hydrophilic, and hydrophobic interactions. Indeed, this has important implications for antibody selection and performance. In order for an effective interaction to occur between the target antigen and the antibody, the epitope must be easy to bind.

Natural antigens usually have multiple antigenic epitopes that stimulate the body to produce multiple specific antibodies. If two different antigenic molecules have the same or similar antigenic epitopes between them, the two antigens stimulate the body to produce antibodies (antisera) that react not only with the specific binding of the antigen that induced their production but also with other antigens that contain the same or similar antigenic epitopes.

In addition, in the specific experimental operation, it is necessary to strictly comply with the experimental requirements and control the experimental process and steps to ensure that the epitope will not be changed. This is because fixation, reduction, pH changes, or gel electrophoresis preparation may result in denaturation of the antigen and consequent epitope changes. This can further contribute to the ability of the antigen to interact with the antibody. For example, some antibodies are ineffective in protein blotting (WB) but are suitable for immunohistochemistry (IHC) applications because complex antigenic sites may be retained in tissues in IHC procedures, whereas in WB procedures the sample preparation process is sufficiently altered to alter the protein conformation to disrupt the antigenic sites, thereby eliminating antibody binding.

Creative Biolabs has a wealth of knowledge and experience in premade antibody library screening. We would be happy to share with you our knowledge and experience in premade phage displayed human antibody library construction and anti-epitope antibody discovery.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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