Description: Human IL-1 beta, also called lymphocyte activating factor (LAF), endogenous pyrogen (EP), leucocyte endogenous mediator (LEM), mononuclear cell factor (MCF), is produced by a wide variety of cells, including macrophages, dendritic cells, T cells and B cells. IL-1 beta is mostly released and has only 20% amino acid homology with IL-1 alpha. The immune regulatory role of IL-1\beta is exerted on a wide range of cells including lymphocytes, epithelial cells and fibroblasts.In vivo, it induces hypotension, fever, and acute phase response.
Applications Reported: Recombinant human IL-1 beta is biologically active. The protein is reported for use in bioassay and as the standard for ELISA.
Applications Tested: The ED50 of this protein, as measured by D10S cell proliferation assay, is less than or equal to 125 pg/mL. This corresponds to a specific activity of greater than or equal to 8 x 10e6 Units/mg.
Source: E. coli expressed amino acids Ala117-Ser269 of human IL-1 beta accession # NM_000576.
Bioactivity: The ED50 of this protein, as measured by D10S cell proliferation assay, is less than or equal to 125 pg/mL. This corresponds to a specific activity of greater than or equal to 8 x 10e6 Units/mg.
Endotoxin: Less than 0.01 ng/ug cytokine as determined by the LAL assay. Purity: >98% as determined by SDS-PAGE.
Molecular Weight: The protein is not methionylated at the N-terminal and has a predicted molecular mass of 17,377. The DTT reduced and non-reduced proteins migrate as 18 kDa polypeptides on SDS-PAGE.
Storage and handling: For best recovery, quick-spin vial prior to opening. Use in a sterile environment.
Interleukin-1 beta (IL-1 beta) is a proinflammatory cytokine expressed by monocytes, macrophages, and dendritic cells. It 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 instead 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. These cytokines play important roles in innate host defense by triggering the production of other proinflammatory cytokines in target cells and initiating acute-phase responses. Their 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. Elevated levels of IL-1 beta have been associated with many chronic inflammatory conditions, giving IL-RA or IL-1 beta neutralizing antibodies potential therapeutical value.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Catabolin; IL-1 beta; interleukin 1, beta; Interleukin-1 beta; preinterleukin 1 beta; pro-interleukin-1-beta
Gene Aliases: IL-1; IL1-BETA; IL1B; IL1F2
UniProt ID: (Human) P01584
Entrez Gene ID: (Human) 3553