Antibody light chains are important components of immunoglobulins (Ig) contributing to antigen recognition, antibody diversity, and the overall structure of antibodies. Like heavy chains, antibody light chains undergo gene rearrangement during B cell development. There are two types of light chains: kappa (κ) and lambda (λ). The recombination of variable (V), joining (J), and constant (C) gene segments results in the diverse variable region of the light chain (VL). Antibody light chains consist of domains that contribute to the structure and function of the antibody. The variable domain (VL) of the light chain contains three complementarity-determining regions (CDRs), which are essential for antigen binding. However, unlike heavy chains, antibody light chains do not have distinct isotypes or subclasses. Both κ and λ light chains can associate with different heavy chain classes to form various antibody isotypes (e.g., IgG, IgM, IgA). Antibody light chains are synthesized on cytoplasmic ribosomes in B cells. After synthesis, they are translocated into the endoplasmic reticulum (ER), where they undergo proper folding with the assistance of chaperone proteins. During folding, cysteine residues within the light chain polypeptide chain come into proximity, allowing them to form disulphide bonds through an oxidation reaction. Disulphide bonds within the light chain contribute to the overall stability of antibodies. They also help maintain the structural integrity of the antigen-binding site and the interaction between the light and heavy chains. The variable region of the light chain, together with the variable region of the heavy chain, forms the antigen-binding site of the antibody. The diversity of light chain variable regions contributes to the ability of antibodies to recognize and bind to a large variety of antigens. The hinge region between the variable and constant domains of the light chain contributes to the flexibility of the antibody molecule. This flexibility is crucial for the proper orientation of the antigen-binding sites and optimal antigen recognition. Although light chains do not have isotypes, the choice of light chain isotype can influence the overall antibody function. Kappa (κ) light chains are more commonly found in antibodies with around 60-70% of antibodies possessing kappa light chains. The type of light chain used (kappa or lambda) does not significantly affect the overall function of the antibody or its ability to recognize and bind antigens. However, the differences in amino acid sequences between kappa and lambda light chains result in different potential antigen-binding specificities. This may therefore contribute to the diversity of the antibody repertoire. Different light chain isotypes may also interact differently with the constant regions of heavy chains, affecting the antibody's effector functions. Antibody light chains associate with antibody heavy chains to form the complete antibody molecule. The correct assembly of light and heavy chains is essential for the stability and functionality of antibodies. Overall, light chains contribute significantly to antibody diversity, allowing B cells to produce antibodies with diverse antigen specificities. This diversity enables the immune system to respond to a wide variety of pathogens. We offer a comprehensive product catalogue of research reagents for investigating immunoglobulin light chains, including Kappa light chain antibodies, Lambda Light chain antibodies, Human Kappa Light Chain antibodies, and IGLL1 antibodies. Explore our full immunoglobulin light chains product range below and discover more, for less. Alternatively, you can explore our Kappa and Lambda product ranges.