Antigen
Antigens are "targeted" by antibodies. Each antibody is specifically produced by the immune system to match an antigen after cells in the immune system come into "contact" with it; this allows a precise identification or matching of the antigen and the initiation of a tailored response. The antibody is said to "match" the antigen in the sense that it can bind to it due to an adaptation in a region of the antibody; because of this, many different antibodies are produced, each able to bind a different antigen while sharing the same basic structure. In most cases, an adapted antibody can only react to and bind one specific antigen; in some instances, however, antibodies may cross-react and bind more than one antigen.
Snake antivenom
Compositions of the antivenom can be classified as whole IgG, or fragments of IgG. Whole antibody products consist of the entire antibody molecule, often immunoglobulin G (IgG), whereas antibody fragments are derived by digesting the whole IgG into Fab (monomeric binding) or F(ab')2 (dimeric binding). The fragment antigen binding, or Fab, is the selective antigen binding region. An antibody, such as IgG, can be digested by papain to produce three fragments: two Fab fragments and one Fc fragment. An antibody can also be digested by pepsin to produce two fragments: a F(ab') fragment and a pFc' fragment.
The fragment antigen-binding (Fab fragment) is a region on an antibody that binds to antigens, such as venoms. The molecular size of Fab is approximately 50kDa, making it smaller than F(ab') which is approximately 110kDa. These size differences greatly affect the tissue distribution and rates of elimination.