Description: The B122 antibody reacts with mouse and rat interleukin-1beta (IL-1beta), a 17 kDa factor secreted primarily by monocytes. IL-1 has effects on T-helper cells, inducing IL-2 secretion and expression of IL-2 receptors. Applications Reported: The B122 antibody has been reported for use in cytokine neutralization and ELISA capture. Applications Tested: The Functional Grade Purified B122 antibody has been tested by LAL assay to verify low endotoxin levels, by ELISA, and in bioassay for neutralization of mouse IL-1 beta bioactivity. The B122 antibody at 0.125 µg/mL has been found to inhibit by 50% the biological effects of 4.0 ng/mL mouse IL-1 beta in a D10 cell proliferation assay. Detailed information and protocols about cytokine bioassays and in vitro cytokine neutralization using antibodies can be found in the BestProtocols® section. The B122 antibody has been tested as the capture antibody in a sandwich ELISA for analysis of mouse interleukin-1 beta (IL-1 beta) in combination with the biotin anti-mouse Interleukin-1 beta (IL-1 beta) polyclonal (13-7112) antibody for detection and recombit mouse IL-1 beta (14-8012) as the standard. A suitable range of concentrations of this antibody for ELISA capture is 1-4 µg/mL. A standard curve consisting of doubling dilutions of the recombit standard over the range of 2000 pg/mL - 15 pg/mL should be included in each ELISA plate. Endotoxin: Less than 0.001 ng/ug antibody as determined by the LAL assay. Storage and handling: Use in a sterile environment. Filtration: 0.2 µm post-manufacturing filtered. Purity: Greater than 90%, as determined by SDS-PAGE. Endotoxin Level: Less than 0.001 ng/µg antibody, as determined by LAL assay. Aggregation: Less than 10%, as determined by HPLC. Interleukin-1 beta (IL-1 beta) is a proinflammatory cytokine expressed by monocytes, macrophages, and dendritic cells. IL-1 beta is synthesized in response to inflammatory stimuli as a 31 kDa inactive pro-form that accumulates in the cytosol. Cleavage of pro-IL-1 beta into the active 17 kDa protein requires the activation of inflammasomes, which are multi-protein complexes that respond to pathogens, stress conditions, and other danger signals. Inflammasome activation triggers the processing of the caspase-1 precursor into its active form, which in turn cleaves pro-IL-1 beta. IL-1 beta lacks a signal sequence peptide for classical ER/Golgi pathway and is secreted alongside caspase-1 via an alternate and incompletely understood mechanism. Although IL-1 beta is most often secreted in its active form, secretion of the uncleaved protein may be detectable under some biological conditions. IL-1 beta signals through two receptors, IL-1RI and IL-1RII, both of which are shared with IL-1 alpha. IL-1 beta activity can be moderated by IL-1 Receptor Antagonist (IL-1RA), a protein produced by many cell types that blocks receptor binding through competitive inhibition. IL-1 beta play an important role in innate host defense by triggering the production of other proinflammatory cytokines in target cells and initiating acute-phase responses to infection and injury. Elevated levels of IL-1 beta have been associated with many chronic inflammatory conditions IL-1 beta neutralizing antibodies potential therapeutic value.
|ELISA, Functional Assay, Neutralization|
|PBS with no preservative; pH 7.2|
For Research Use Only.
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