Ig Lambda Constant 2 Protein, Human (HEK293, His)

The constant region of immunoglobulin light chains, specifically Ig Lambda Constant 2 protein, is integral to the structure of antibodies, also known as immunoglobulins. These membrane-bound or secreted glycoproteins are produced by B lymphocytes and function as receptors in the recognition phase of humoral immunity. Upon binding a specific antigen, membrane-bound immunoglobulins instigate the clonal expansion and differentiation of B lymphocytes into plasma cells that secrete immunoglobulins. Secreted immunoglobulins, in turn, play a pivotal role in the effector phase of humoral immunity, facilitating the elimination of bound antigens. The antigen binding site is orchestrated by the variable domain of one heavy chain, coupled with that of its associated light chain, resulting in each immunoglobulin possessing two antigen binding sites with remarkable affinity for a particular antigen. The variable domains undergo V-(D)-J rearrangement and subsequent somatic hypermutations, enabling affinity maturation after exposure to antigen and selection. Immunoglobulins are composed of two identical heavy chains and two identical light chains, interconnected by disulfide linkages.