Product Pathways - Growth Factors/Cytokines
Mouse Interleukin-1α (mIL-1α) #5273
PhosphoSitePlus® protein, site, and accession data: IL1A
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Source
Recombinant mouse IL-1α (mIL-1α) Ser115-Ser270 (Accession #NP_034684) was produced in E.coli at Cell Signaling Technology.
Molecular Characterization
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.
Purity
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant mIL-1α. All lots are greater than 98% pure.
Bioactivity
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 3-8 pg/ml.
Coomassie Gel
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.
Bioactivity
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.
Western Blotting
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).
Endotoxin
Less than 0.01 ng endotoxin/1 μg mIL-1α.
Formulation
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.
Background
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).
- Dinarello, C.A. (1996) Blood 87, 2095-147.
- Allan, S.M. et al. (2005) Nat Rev Immunol 5, 629-40.
- Di Paolo, N.C. et al. (2009) Immunity 31, 110-21.
Application References
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Companion Products
- 9215 Phospho-p38 MAPK (Thr180/Tyr182) (3D7) Rabbit mAb
- 9212 p38 MAPK Antibody
- 9872 Phosphate Buffered Saline (PBS-1X) pH7.2 (Sterile)
For Research Use Only. Not For Use In Diagnostic Procedures.
