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The protein G and the related protein A support binding of the antibody at the Fc region, which orients the antibody with the antigen-binding sites away from the surface and toward the solution.
To this end, protein A plays a multifaceted role: By binding the Fc portion of antibodies, protein A renders them inaccessible to the opsonins, thus impairing phagocytosis of the bacteria via immune cell attack. Protein A facilitates the adherence of S.
The large protein (L) is the enzymatic component of the LP polymerase complex and is responsible for nucleotide addition to the neosynthesized RNA chain (RdRp activity) and for the synthesis of the cap-structure for the viral mRNAs.
Antibody binding proteins such as Protein A and Protein G are often used in antibody purification and in applications such as immunoprecipitation (IP) and chromatin immunoprecipitation (ChIP). Each antibody binding protein varies in its ability to bind to antibodies of different subtypes and species.
Protein G consists of an N-terminal signal sequence (Ss), an albumin-binding region containing three albumin-binding domains and a C-terminal immunoglobulin-binding region. A spacer (S) separates the binding regions and a C-terminal sequence (W) anchors the protein to the cell wall.
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Protein A and protein G bind with high affinity and specificity to Fc region of immunoglobulins from many of mammalian species, most notably IgGs. Unlike protein A and G, Protein L binds immunoglobulins through kappa light chain. These proteins have been usually used to purify, immobilize or detect immunoglobulins.
Protein A and protein G bind with high affinity and specificity to Fc region of immunoglobulins from many of mammalian species, most notably IgGs. Unlike protein A and G, Protein L binds immunoglobulins through kappa light chain. These proteins have been usually used to purify, immobilize or detect immunoglobulins.
Secondly, protein G is able to bind to Fab as well as to Fc. Although the constant domains of Fab and Fc are structurally related, they are recognized by protein G in quite different ways. Protein G binds edge-on to the CH 1 domain in Fab, but recognizes Fc by binding in a cleft between CH 2 and CH 3 domains.

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