CD40L (mouse) (multimeric) (rec.) (Biotin)

The costimulatory molecule CD40, a member of the tumor necrosis factor (TNF) receptor superfamily, critically regulates B cell and T cell function in adaptive immunity and inflammation by interacting with CD40L (CD154). CD40L mediates a range of activities on B cells, including induction of activation-associated surface antigen, entry into cell cycle, isotype switching, immunoglobulin secretion and memory generation. CD40-CD40L interaction also plays important roles in monocyte activation and DC maturation. MultimericCD40L(TM) is a high activity construct in which two trimeric CD40 ligands are artificially linked via the collagen domain of ACRP30. This construct very effectively simulates the natural membrane-assisted aggregation of CD40L in vivo. It provides a simple and equally potent alternative to CD40L+enhancer combinations. MultimericCD40L(TM) has shown to suppress alum-induced IL-1beta release and caspase-1 activation in a dose-, CD40- and time dependent manner, without affecting BMDM (bone marrow-derived macrophages) viability. It also effectively suppressed the inflammasome function triggered by NLRP3 activators. The secretion of caspase-1 independent inflammatory mediators has been shown to be unaltered or even enhanced. MultimericCD40L(TM) enhances B cell proliferation. Protein function: Cytokine that acts as a ligand to CD40/TNFRSF5. Costimulates T-cell proliferation and cytokine production. Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation. Induces the activation of NF-kappa-B. Induces the activation of kinases MAPK8 and PAK2 in T-cells. Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (PubMed:1374165). Involved in immunoglobulin class switching (PubMed:1374165). [The UniProt Consortium]