Immunoglobulin lambda variable 2-18 (IGLV2-18)

Immunoglobulin lambda variable 2-18 (IGLV2-18) is a variable (V) region segment of the immunoglobulin lambda light chain, which forms part of antibodies produced by B lymphocytes. The protein encodes the variable domain of the immunoglobulin light chain, responsible for the antigen recognition properties of antibodies. The variable domain, in combination with a heavy chain variable domain, forms the antigen-binding site of an antibody, allowing the immune system to specifically recognize and bind to a broad variety of antigens. The diversity of these variable regions is generated by V-(D)-J recombination during B cell development and further increased by somatic hypermutation after antigen exposure. IGLV2-18 is thus not a classical therapeutic target like a receptor or enzyme, but rather a genetic element contributing to antibody diversity and function essential for adaptive immunity[1][2][3][4][5][8]. Additional details: - IGLV2-18 is predicted to be expressed on the extracellular region and plasma membrane as part of the immunoglobulin complex[1]. - Certain genetic variations in IGLV2-18 have been associated with autism spectrum disorder in some studies, but it is not a primary disease gene nor a common direct drug target[1]. - There are no known drugs directly interacting with IGLV2-18, nor is it a known biomarker or therapeutic target in the conventional sense. - The gene is annotated in major genomic databases such as HGNC (5889), NCBI Gene (28814), and Ensembl (ENSG00000211664)[1][6][7]. IGLV2-18 primarily functions as a genetic and protein element of the adaptive immune system's antibody response, contributing to the capacity of antibodies to recognize and bind specific antigens[2][8].

Other names

Immunoglobulin lambda variable 2-18IGLV2-18IGLV218V1-5