cases, the process relies on physical binding between pools of antibodies and the antigen, followed by sequencing of the variable regions of heavy and light chains. These are then expressed from cDNA clones as recombinant proteins.
Antibody fragments, which consist only of the variable regions responsible for antigen recognition without the additional scaffold regions of a four-chain antibody, can also be cloned. These fragments are shorter and sometimes encoded within a single exon. Protein scientists at Allele have developed a powerful method to clone such antibody fragments with exceptional efficiency, without requiring any physical antigen binding. This innovation, which was awarded a U.S. patent this week, leverages the immune system’s own natural selection and expansion processes. By applying deep sequencing at the gene and protein level and ranking enriched sequences, Allele can generate a large collection of naturally optimized binders since the host immune system has already selected and refined them. The patent also claims the use of this technology for selecting T-cell receptors (TCRs).
This breakthrough aligns seamlessly with one of Allele Reagents’ core platforms, the nanoantibody (nAb) reagent family. This reagent line includes nAb-beads, which enable highly convenient and clean co-immunoprecipitation, as well as intrabodies, compact ~14 kDa antibodies that can be expressed inside cells to target intracellular antigens. When combined with Allele’s mRNAExpress platform, the power and versatility of these tools are further amplified.
