Camelids produce functional IgG isotypes that do not incorporate light chains. Comparative studies of old world camelids (Camelus bactrianus and Camelus dromedarius) and new world camelids (Lama pacos, Lama glama and Lama vicugna) have shown that heavy-chain-only immunoglobulins represent between 35% – 70% of total IgG in the sera of all species. At present, three subclasses of camelid IgG have been identified (IgG1, IgG2, IgG3), of which IgG2 and IgG3 lack the light chains. IgG1 binds strongly to protein A and G, is composed of conventional antibodies, and totals 25 % of serum IgG. Llama IgG1 antibodies migrate as a 150-kDa protein in SDS-polyacrylamide gel under non-reducing conditions. Under reducing conditions, IgG1 antibodies split into four proteins (two of each H- and L-chains), which gives protein bands of about 52-55 kDa (H-chain) and about 27 kDa (L-chain). Anti-Llama IgG1 generated in rabbit detects specifically the Llama IgG1 isotype. This anti-Llama secondary Antibody is suitable for western blot, ELISA, ChIP and immunohistochemistry as well as other more general immunoassays.
