How many complementarity-determining regions (CDRs) are present in an IgG molecule?

How many complementarity-determining regions (CDRs) are present in an IgG molecule? Correct Answer Twelve

Twelve complementarity-determining regions (CDRs) are present in an IgG molecule. There are three CDRs in each of the L and H chains and these six CDRs fold to form the antibody binding site. As there are two antigen-binding sites on an antibody molecule, the total number of CDRs in an antibody is twelve. These CDRs form loops, which are located at one end of the V domains.
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Which one of the combinations of the following statements is true about antibody structure?
P. Limited proteolysis of rabbit IgG with the enzyme pepsin generates two antigen-binding regions (Fab) and an Fc fragment.
Q. Limited proteolysis of rabbit IgG with the enzyme papain generates a single bivalent antigen-binding region F(ab')2 and peptide fragments.
R. The Fc fragment of IgG can self-associate and crystallize into a lattice.
S. The F(ab')2 fragment of IgG is composed of both light and heavy chains.
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