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Mouse Interleukin-1α (mIL-1α)

Mouse Interleukin-1α (mIL-1α) #5273

This product is discontinued

Coomassie Gel Image 1

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.

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Bioactivity Image 2

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.

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Western Blotting Image 3

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).

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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.

Molecular Formula:

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).

  1. Dinarello, C.A. (1996) Blood 87, 2095-147.
  2. Allan, S.M. et al. (2005) Nat Rev Immunol 5, 629-40.
  3. Di Paolo, N.C. et al. (2009) Immunity 31, 110-21.
Entrez-Gene Id
Swiss-Prot Acc.
For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

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