Anti-Human C1q Monoclonal Antibody (clone JL-1) -100 µg (CAT#: CB-P147-AB) Datasheet

Antibody

The monoclonal antibody JL-1 recognizes the collagen-like region (CLR) of human C1q. It is a 459 kDa molecule composed of three independent polypeptide chains. The antibody is immunized with purified mouse C1q-/-C57BL / C1q produced by 6 mice.
C1q together with C1r and C1s form the first part of the classical complement pathway, C1 macromolecules. The interaction between the immune complex and C1q induces conformational changes in the C1 complex, thereby activating the classical pathway. C1q acts as a recognition unit by binding to the heavy chain of IgG or IgM (Fcγ and Fc micro), provided that the immunoglobulin binds to its antigen. In addition, C1q can also recognize molecular patterns associated with pathogens, and can bind to apoptotic vesicles, thereby activating the classical complement pathway and mediating phagocytosis. In this way, C1q promotes the clearance of apoptotic cells and subsequent exposure of self-antigens, thereby preventing stimulation of the immune system.
C1q is mainly produced by macrophages, but also by follicular dendritic cells, finger cells and cells of the mononuclear macrophage lineage. C1q deficiency has a profound impact on host defense and immune complex clearance. Lack of C1q may lead to impaired clearance rate of apoptotic cells, leading to autoimmunity. Hereditary C1q deficiency is also associated with the development of systemic lupus erythematosus (SLE).
The monoclonal antibody JL-1 only reacts with the collagen-like region (CLR), which is the same region that mouse and human autoantibodies bind. Anti-C1q autoantibodies are deposited in the glomerulus together with C1q, but only in the case of glomerular immune complex disease can it induce obvious kidney disease. This explains why anti-C1q antibodies are particularly pathogenic in SLE patients.

Nephrology, Neurological disorders