Function
Immunoglobulin heavy chain constant regions are integral components of immunoglobulins, also known as antibodies. These glycoproteins are either membrane-bound or secreted and are produced by B lymphocytes. In humoral immunity, membrane-bound immunoglobulins act as receptors. Upon binding to a specific antigen, they trigger the clonal expansion and differentiation of B lymphocytes into plasma cells, which secrete immunoglobulins. Secreted immunoglobulins play a crucial role in the effector phase of humoral immunity, leading to the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with its associated light chain. Consequently, each immunoglobulin possesses two antigen binding sites with remarkable affinity for a specific antigen. The variable domains are assembled through a process called V-(D)-J rearrangement and can subsequently undergo somatic hypermutations. These mutations, after exposure to antigen and selection, contribute to affinity maturation for a particular antigen. Ig alpha is the predominant immunoglobulin class found in bodily secretions.