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The fragment crystallizable region (Fc region) is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This region allows antibodies to activate the immune system , for example, through binding to Fc receptors .
Fcabs are antibodies fragments engineered from the constant region of an antibody . [1] In naturally occurring antibodies (such as IgGs ), the antigen-binding sites are located at the variable regions (Fab).
The universal structure of antibody includes the constant regions part of the fragment crystallizable(Fc) region of the antibody (shown in dark blue). It also includes the fragment antigen binding which is composed of one heavy and one light chain (shown as L for light and H for heavy).
In an experimental setting, Fc and Fab fragments can be generated in the laboratory. The enzyme papain can be used to cleave an immunoglobulin monomer into two Fab fragments and an Fc fragment. Conversely, the enzyme pepsin cleaves below the hinge region, so the result instead is a F(ab') 2 fragment and a pFc' fragment.
In an antibody, the Fab (fragment, antigen-binding) region is formed from the amino-terminal end of both the light and heavy chains of the immunoglobulin polypeptide. This region, called the variable (V) domain, is composed of amino acid sequences that define each type of antibody and their binding affinity to an antigen.
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An antibody fragment can be: a fragment antigen-binding (Fab) a fragment crystallizable (Fc) This page was last edited on 14 May 2022 ...
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