The purity of recombinant mIL-1α was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant mIL-1α and staining overnight with Coomassie Blue.Learn more about how we get our images
The production of mouse IL-6 by 3T3 MEFs WT cultured with increasing concentrations of mIL-1α was assessed. Media from cells incubated with mIL-1α for 24 hours was collected and assayed for mouse IL-6 by ELISA and the OD450-OD650 was determined.Learn more about how we get our images
Western blot analysis of extracts from 3T3 MEFs WT untreated or treated with mIL-1α for 10 minutes, using Phospho-p38 MAPK (Thr180/Tyr182) (3D7) Rabbit mAb #9215 (upper) and p38 MAPK Antibody #9212 (lower).Learn more about how we get our images
Recombinant mouse IL-1α (mIL-1α) Ser115-Ser270 (Accession #NP_034684) was produced in E.coli at Cell Signaling Technology.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant mIL-1α. All lots are greater than 98% pure.
Recombinant mIL-1α does not have a Met on the amino terminus and has a calculated MW of 17,990. DTT-reduced and non-reduced protein migrate as 18 kDa polypeptides. The expected amino-terminus SAPYT of recombinant mIL-1α was verified by amino acid sequencing.
The bioactivity of recombinant mIL-1α 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.
Less than 0.01 ng endotoxin/1 μg mIL-1α.
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 20 μg BSA per 1 μg mIL-1α. Carrier free: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2.
Stable in lyophilized state at 4°C for 1 year after receipt. Sterile stock solutions reconstituted with carrier protein are stable at 4°C for 2 months and at -20°C for 6 months. Avoid repeated freeze-thaw cycles.Maintain sterility. Storage at -20°C should be in a manual defrost freezer.
IL-1α is a pro-inflammatory cytokine produced by activated monocytes, lymphocytes and epithelial cells (1). IL-1α is synthesized as an active precursor protein that appears to be cleaved by cytosolic proteases into its mature form (1,2). Often, precursor and mature forms of IL-1α are primarily retained intracellularly rather than constitutively secreted. (1,2). Signaling by IL-1α involves IL-1α binding to an 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 NFκB pathways (1,2). IL-1α also binds to an IL-RII that lacks an intracellular signaling domain and thereby serves as a high affinity decoy receptor. Inhibition of IL-1α activity is through IL-1R antagonist (IL-1Ra) that binds IL-1R1 but does not signal. IL-1α has been shown to be a key mediator of virus-induced inflammatory responses in mice (3).
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