The 187.1 monoclonal antibody reacts with the kappa chain of the mouse immunoglobulin light chain. The κ chain is one of two types of polypeptide subunits which make up the immunoglobulin light chain. A typical antibody is composed of two immunoglobulin heavy chains and two immunoglobulin light chains. The κ chain is coded for by V (variable J (joining) and C (constant) genes. These genes undergo V(D)J recombination to generate a diverse repertoire of immunoglobulins.'

InVivoMAb anti-mouse Kappa Immunoglobulin Light Chain (Clone: 187.1 (HB58))

 Burbage, M., et al. (2015). "Cdc42 is a key regulator of B cell differentiation and is required for antiviral humoral immunity." J Exp Med 212(1): 53-72. PubMed

The small Rho GTPase Cdc42, known to interact with Wiskott-Aldrich syndrome (WAS) protein, is an important regulator of actin remodeling. Here, we show that genetic ablation of Cdc42 exclusively in the B cell lineage is sufficient to render mice unable to mount antibody responses. Indeed Cdc42-deficient mice are incapable of forming germinal centers or generating plasma B cells upon either viral infection or immunization. Such severe immune deficiency is caused by multiple and profound B cell abnormalities, including early blocks during B cell development; impaired antigen-driven BCR signaling and actin remodeling; defective antigen presentation and in vivo interaction with T cells; and a severe B cell-intrinsic block in plasma cell differentiation. Thus, our study presents a new perspective on Cdc42 as key regulator of B cell physiology.