PeproTech IL18BP Polyclonal Antibody, Biotin, PeproTech®, Invitrogen™

Descripción

Preparation: Produced from sera of goats immunized with highly pure Recombinant Murine IL-18BP. Anti-Murine IL-18BP-specific antibody was purified by affinity chromatography and then biotinylated. Sandwich ELISA: To detect Murine IL-18BP by sandwich ELISA (using 100 μL/well antibody solution) a concentration of 0.25-1.0 μg/mL of this antibody is required. This biotinylated polyclonal antibody, in conjunction with PeproTech Polyclonal Anti-Murine IL-18BP (500-P153G) as a capture antibody, allows the detection of at least 0.2-0.4 ng/well of Recombinant Murine IL-18BP. Western Blot: To detect mIL-18BP by Western Blot analysis this antibody can be used at a concentration of 0.1-0.2 μg/mL. Used in conjunction with compatible secondary reagents the detection limit for Recombinant mIL-18BP is 1.5-3.0 ng/lane, under either reducing or non-reducing conditions. 500-P153GBT-1MG will be provided as 2 x 500 μg

Interleukin-18 binding protein (IL-18BP) is a constitutively secreted glycoprotein that acts as a natural antagonist for interleukin-18 (IL-18) by preventing interaction between IL-18 and its receptors. Through this binding, IL-18BP neutralizes the proinflammatory role of IL-18 in cell-mediated immune responses, resulting in reduced IFN-gamma production by T helper type I cells and inhibition of allospecific cytotoxic T lymphocyte (CTL) activity through augmented natural killer (NK) cell cytotoxicity. As an inhibitor of IL-18 and an essential component of skin homeostasis, IL-18BP has been linked to a variety of diseases, including eczema, asthma, and the autoimmune condition, Crohn's disease. The upregulation of IL-18BP by keratinocytes expressing the human papillomavirus (HPV) E7 oncoprotein has been shown to decrease IL-18-induced IFN-gamma production and IL-18-mediated T cell activation. Elevated levels of IL-18 and IL-18BP, as well as proinflammatory cytokines IFN-gamma, TNF-alpha, IL-1beta and IL-8, have been linked to chronic inflammation and observed in macrophages (including Kupffer cells) isolated from lesions and intestinal tissues of Crohn's disease patients. As a member of the immunoglobulin-like class of receptors, IL-18BP contains a single immunoglobulin (Ig) domain; although two (b and d) of the four identified human isoforms (a-d) contain incomplete domains that greatly reduce their binding affinity.