|Purity||>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant mIL-1β. All lots are greater than 98% pure.|
|Endotoxin||Less than 0.01 ng endotoxin/1 μg mIL-1β.|
|Activity||The bioactivity of recombinant mIL-1β was determined by its ability to induce mouse IL-6 production by 3T3 MEFs WT. The ED50 of each lot is between 5-20 pg/ml.|
|Molecular Formula||Recombinant mIL-1β has a Met on the amino terminus and has a calculated MW of 17,525. DTT-reduced and non-reduced protein migrate as 18 kDa polypeptides. The expected amino-terminal MVPIR of recombinant mIL-1β was verified by amino acid sequencing.|
Recombinant mouse IL-1β (mIL-1β) Val118-Ser269 (Accession #NP_032387) was produced in E.coli at Cell Signaling Technology.
IL-1β is a pro-inflammatory cytokine produced predominantly by activated monocytes and epithelial cells (1). Precursor IL-1β is cleaved by caspase-1 and mature IL-1β is then secreted (1-3). Target cells include macrophages and many other cell types. Signaling by IL-1β involves IL-1β binding to IL-1 accessory protein (IL-1-AcP) and then the complex binds to IL-1RI (1,2). Signaling is through activation of MAP kinase and NF-κB pathways (1,2). IL-1β also binds to IL-1RII that lacks an intracellular signaling domain and thereby serves as a high affinity decoy receptor. IL-1β binding to IL-1RI is inhibited by the negative regulator, IL-1R antagonist (IL-1Ra). IL-1Ra binding to IL-1RI does not signal and serves to block IL-1β signaling. IL-1β plays critical roles in the acute phase response and sepsis (1-3).
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