Immunoglobulin lambda variable 3-27 (IGLV3-27)

Immunoglobulin lambda variable 3-27 is a protein encoded by the IGLV3-27 gene that forms part of the variable (V) region of the immunoglobulin (Ig) lambda light chain. This region participates in antigen recognition and is fundamental to antibody diversity, enabling B lymphocytes to detect a wide array of pathogens. Like all immunoglobulin variable domains, IGLV3-27 is involved in the creation of the antigen-binding site and contributes to the adaptive immune response. It is not a direct therapeutic target or receptor but rather a component of antibody structure used by the immune system for specific antigen binding[1][3][4][5][6].\n\n**Context and supporting detail:**\n- **Immunoglobulin light chains** (lambda and kappa) contain variable regions, and IGLV3-27 encodes one specific variant of these domains[1][2][4][5].\n- **Function**: It is part of the mechanism by which antibodies recognize diverse antigens as part of the humoral immune response, but not directly "targeted" by drugs or considered a receptor or enzyme[4][5][6].\n- **Expression**: Expressed as part of B lymphocyte antibody diversification[7].\n- **Clinical Relevance**: No direct drug interactions or biomarker information is associated; not considered an actionable therapeutic molecular target but fundamental to adaptive immunity[3][6].\n- **Aliases**: Variants stem from historical nomenclature for immunoglobulin regions and sequencing projects, all denote the same variable region gene.\n\n**Explanation**:\nIGLV3-27 is a variable domain gene segment and not a druggable target or receptor. Its significance is biological, underpinning how antibodies gain specificity for antigens, thus enabling immune system diversity[1][3][4][5].

Other names

Immunoglobulin lambda variable 3-27IGLV3-27Ig lambda chain V-IV region KernIGLV327V2-19