What is the Fc region?

The Fc region, also known as the fragment crystallizable region, is a region of an antibody molecule that is responsible for binding to various immune cells and proteins. It plays a crucial role in the immune response by mediating the effector functions of antibodies, such as antibody-dependent cell-mediated cytotoxicity (ADCC), complement activation, and phagocytosis. The Fc region is located at the tail end of the antibody molecule and is constant in structure within a particular class of antibodies (e.g. IgG, IgA, IgM, etc.).

The Fc region, also known as the fragment crystallizable region, is a portion of the antibody molecule that is responsible for binding to specific receptors on immune cells, triggering immune responses. It is found in the constant region of the antibody and is composed of the CH2 and CH3 domains. The Fc region's structure and sequence vary depending on the antibody's class and subclass, which influence the specific effector functions and interactions with immune cells.