Antibody purification using antibody-binding proteinsWritten/Edited by Rene von der Forst, MSE
Protein A, protein G, and Protein L are native and recombinant proteins of microbial origin that bind to mammalian immunoglobulins (Ig). Protein A and protein G bind with high affinity and specificity to the Fc region of immunoglobulins from various mammalian species, most notably the IgGs. Protein L binds immunoglobulins via the kappa light chain. These antibody-binding proteins can be used to purify, immobilize or detect immunoglobulins. These proteins (i.e. protein A, protein G, protein L) are typically attached onto a solid support such as sepharose or magnetic beads. Table 1 summarizes the various formats available for the antibody-binding proteins.
Table 1. Formats available for antibody-binding proteins
|Antibody-binding protein||Sepharose beads||Magnetic beads||Sepharose column|
|Protein A / G||ABIN412443||ABIN400577||ABIN629425|
|Protein A / G / L||ABIN412465||ABIN412469||ABIN629429|
Mammalian immunoglobulin (Ig) can be purified from cell culture media, ascites and serum samples. These antibody-protein bound beads offer a convenient method to achieve high purity and high recovery of monoclonal and polyclonal antibodies from various biological samples. Naturally, the binding specificities and affinities of these proteins would vary between source species and antibody subclass. Table 2 summarizes the antibody binding specificities of each antibody-binding protein for human, mouse and rat.
Table 2. Protein A / G / L binding affinities for immunoglobulins
|Species||Immunoglobulin||Protein A||Protein G||Protein L|
Note: H = human, M = mouse, R = rat
Master of Science in engineering. 12+ years of experience in marketing and e-commerce in the life science sector.Go to author page