Bio-Synthesis has branched into several related areas such as DNA paternity testing, DNA HLA typing, PNA's, genomic sequencing, fluorescence based genotyping, custom organic synthesis and other molecular biology based applications. It has maintained its position as an aggressive, innovative company in a highly competitive marketplace without sacrificing quality. Today,newer technologies,such as synthesis of gene construction, PCR, mutagenesis, combinatorial libraries, dye/adduct labeling, DNA micro arrays, peptide-nucleic acid chimerics, etc, have challenged the molecular biology field.
Well-designed anti-peptide antibodies provide the specificity and control for everyday and cutting-edge applications. Pragmatic peptide antigen design principles can be used to help ensure production of successful antibodies. Selective antibodies are powerful tools of experimental biology. Relatively straightforward immune blotting experiments can be used to identify a polypeptide antigen in a novel cell or tissue or to study cellular processing of a precursor protein that is required for biologic activity or targeting. Natural proteins are perhaps the ideal antigens, providing sequence-specific and surface structural epitopes. However, natural proteins are rarely available in completely pure form, and antibodies often develop against contaminating polypeptides. Antibodies against natural proteins, particularly monoclonal antibodies, sometimes have exquisite specificities, recognizing only subsets of the immunizing protein, when a more general reagent was desired.
An epitope, also know as antigenic determinant, is the part of a macromolecule that is recognized by the immune system, specifically by antibodies, B cells, or T cells. The part of an antibody that recognizes the epitope is called a paratope. Although epitopes are usually thought to be derived from non-self proteins, sequences derived from the host that can be recognized are also classified as epitopes. Most epitopes recognized by antibodies or B cells can be thought of as three-dimensional surface features of an antigen molecule; these features fit precisely and thus bind to antibodies. Exceptions are linear epitopes, which are determined by the amino acid sequence (the primary structure) rather than by the 3D shape (tertiary structure) of a protein.