Antibodies are powerful tools for protein and molecular detection and purification. While intact antibodies (typically IgG or IgM) are suitable for most immunoassay applications, certain procedures benefit from the use of antibody fragments such as Fab, scFv, and dAb.

Western blot (WB) is a routine yet powerful protein detection method used to study post-translational modifications, relative protein abundance, molecular weight, and protein-protein interactions. Since its inception, WB has provided valuable insights for academic research, diagnostics, and therapeutic testing. As shown in Figure 1, WB separates native or denatured proteins via gel electrophoresis, transfers them to a membrane while preserving peptide integrity and biological activity, and uses specific antibodies to identify and quantify target proteins within complex mixtures extracted from cells or tissues.

The generation of the VBASE2 database was previously described (Retter et al. 2005).

Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptide – two heavy chains and two light chains joined to form a "Y" shaped molecule.

The Kabat numbering scheme is a widely adopted standard for numbering the residues in an antibody in a consistent manner. However the scheme has problems!