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Immunoglobulin kappa variable 2D-40 is a protein-coding gene segment in the distal cluster of the IGK locus on chromosome 2 (2p11.2) that encodes the variable domain of kappa light chains in human antibodies[3]. Each immunoglobulin molecule consists of two heavy and two light chains (kappa or lambda), with the antigen-binding site formed through the pairing of heavy and light chain variable domains. The IGKV2D-40 gene contributes to antibody diversity via somatic recombination (V-J rearrangement) and hypermutation, which are central to the adaptive immune response. Its genetic variation influences the repertoire and affinity of antibodies produced by B lymphocytes[1][2][3]. It is not considered a drug target but is essential for basic immunological functions and diversity.
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