Description: The CRM56 antibody reacts with human and baboon interleukin-1 beta; (IL-1 beta). IL-1 beta is 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. IL-1 has effects on B cells, promoting cell proliferation and immunoglobulin synthesis. Applications Reported: The CRM56 antibody has been reported for use in cytokine neutralization, and ELISA. Fluorochrome conjugated CRM56 is recommended for use in intracellular staining for flow cytometry. Functional Grade purified CRM56 antibody, cat. 16-7018, is recommended for use in functional assays. Applications Tested: The CRM56 antibody has been tested as the capture antibody in a sandwich ELISA for analysis of human interleukin-1β (IL-1β) in combination with the biotin CRM57 (13-7016) antibody for detection and recombit human IL-1β (14-8018) 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 1000 pg/mL - 8 pg/mL should be included in each ELISA plate. The Functional Grade Purified CRM56 antibody has been tested by LAL assay to verify low endotoxin and by bioassay to verify neutralization of IL-1β bioactivity. For in vitro neutralization, the CRM56 antibody at 2.5 µg/mL has been found to neutralize by 50% the effect of 1 ng/mL human IL-1β bioactivity in a D10.G4.1 cell proliferation bioassay. 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.
|PBS with no preservative; pH 7.2|
|ELISA, Functional Assay, Neutralization|
For Research Use Only.
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