Interleukin 12 (IL-12) is a potent regulator of cell-mediated immune responses. Biologically active IL-12 is secreted by activated B lymphocytes and macrophages as a 70 kD heterodimeric glycoprotein comprised of disulfide-bonded 35 kD (p35) and 40 kD (p40) subunits. The IL-12 p40 monomer shares amino acid sequence homology with the IL-6 receptor. It has been reported that activated PBMC produce a large excess of IL-12 p40 monomer over the bioactive p70 heterodimer. The IL-12 p40 monomer has been reported to inhibit binding of IL-12 p70 to the IL-12 receptor, but with 20X less effectiveness than the IL-12 p40 homodimer. Formulation and Purity : Recombinant mouse IL-12 p40 is supplied as a frozen liquid comprised of 0.22 µm sterile-filtered Dulbecco's PBS (pH 7.2) and no preservatives. The recombinant mouse IL-12, p40 is > 95% pure, as determined by SDS-PAGE, and an absorption assay based on the Beer-Lambert law. The recombinant is not tested for endotoxin or sterility.

(RUO)

40 µg/ml

ELISA Standard (Routinely Tested)

IL-12/IL-23 p40

Frozen aqueous buffered solution containing BSA and glycerol.

Development References(5) 1. D'Andrea A, Aste-Amezaga M, Valiante NM, Ma X, Kubin M, Trinchieri G. Interleukin 10 (IL-10) inhibits human lymphocyte interferon gamma-production by suppressing natural killer cell stimulatory factor/IL-12 synthesis in accessory cells. J Exp Med. 1993; 178(3):1041-1048. (Biology). 2. D'Andrea A, Rengaraju M, Valiante NM, et al. Production of natural killer cell stimulatory factor (interleukin 12) by peripheral blood mononuclear cells. J Exp Med. 1992; 176(5):1387-1398. (Biology). 3. Ling P, Gately MK, Gubler U, et al. Human IL-12 p40 homodimer binds to the IL-12 receptor but does not mediate biologic activity. J Immunol. 1995; 154(1):116-127. (Biology). 4. Schoenhaut DS, Chua AO, Wolitzky AG, et al. Cloning and expression of murine IL-12. J Immunol. 1992; 148(11):3433-3440. (Biology). 5. Zeh HJ III, Tahara H, Lotze MT. Interleukin-12. In: Thomson AW, ed. The Cytokine Handbook. London: Academic Press Limited; 1994:239-256.