Interleukin 1 beta (IL1B) ELISA Overview

IL-1B ELISA (enzyme-linked immunosorbent assay ) is used to determine how much of a target is bound between two antibodies. In the wells of the supplied microplate, a target-specific antibody has been pre-coated. These wells are subsequently filled with samples, standards, or controls, which bind to the immobilized (capture) antibody. The second (detector) antibody is added to the sandwich, followed by a substrate solution that reacts with the enzyme-antibody-target complex to produce a quantifiable signal. The strength of this signal is proportional to the amount of target contained in the original specimen.

Deep dive to Interleukin 1 Beta (IL1B)

Monocytes, macrophages, and dendritic cells all produce interleukin-1 beta (IL-1 beta), which is a proinflammatory cytokine. In response to inflammatory stimuli, IL-1 beta is produced as a 31 kDa inactive pro-form that accumulates in the cytosol. The activation of inflammasomes, which are multi-protein complexes that respond to infections, stress conditions, and other danger signals, is required for cleavage of pro-IL-1 beta into the active 17 kDa protein. When the inflammasome is activated, the caspase-1 precursor is processed into its active form, which then cleaves pro-IL-1 beta. Because IL-1 beta lacks a signal sequence peptide for the traditional ER/Golgi pathway, it is released alongside caspase-1 by an unidentified mechanism. Although most IL-1 beta is released in its active state, it is possible to detect production of the uncleaved protein under certain biological conditions. IL-1 beta communicates with the body through two receptors, IL-1RI and IL-1RII, which are also found in IL-1 alpha. IL-1 Receptor Antagonist (IL-1RA), a protein generated by various cell types that prevents receptor binding through competitive inhibition, can reduce IL-1 beta activity.