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Mouse IL-12 p40 homodimer, amino acids Met23-Ser335 (Accession # NM_008352), was expressed in insect cells.
The 313 amino acid recombinant protein has a predicted molecular mass of 35.8 kD. The DTT-reduced protein migrates at approximately 40 kD and the non-reduced protein migrates at approximately 75 kD by SDS-PAGE. The N-terminal amino acid is Met.
>98%, as determined by Coomassie stained SDS-PAGE.
0.22 µm filtered protein solution is in 20 mM Tris-HCl, pH 8.0, 0.1 M NaCl
Less than 0.01 ng per µg cytokine as determined by the LAL method.
10-100 µg sizes are bottled at 100 µg/mL. 500 µg and larger sizes are bottled at the concentration indicated on the vial.
Storage & Handling:
Unopened vial can be stored at -20°C for six months or at -70°C for one year. For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 µg/mL in sterile buffer containing carrier protein such as 1% BSA or HSA or 10% FBS. Stock solution can be stored for one month at 4°C or up to three months at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
ED50 = 1- 4 ng/ml corresponding to a specific activity of 1.0 - 0.25 x 106 units/mg, as determined by the dose dependent inhibition of IL-12-dependent IFNγ production.
Mouse IL-12 p40 homodimer is able to inhibit IL-12-dependent IFNγ production.
IL-12 and IL-23 share the p40 subunit, which heterodimerizes respectively with IL-12 p35 or IL-23 p19 subunits to form IL-12 or IL-23. IL-12 p40 exists as a monomer and as a homodimer (IL-12 p80). IL-12 induction is relevant in asthmatic airway inflammation. IL-12 expression can be induced by mouse parainfluenza type I (Sendai) virus and its source is airway epithelial cells. In that experimental model, IL-12 induction is followed by excessive expression of IL-12 p40 that could be further enhanced in IL-12 p35-deficient mice. Overexpression of IL-12 p80 causes macrophage accumulation and contributes to airway inflammation and consequent morbidity during viral bronchitis. Amplified epithelial IL-12 p40 expression and augmented concentrations of BAL fluid IL-12 p40 (but not IL-12 p70) has been detected in asthmatic subjects. It has been demonstrated that p80, but not IL-12 or p40, induces macrophage chemotaxis that is independent of IL-12 and mediated through the cytoplasmic tail of IL-12b1. Additional studies with transgenic mice suggest that overexpression of IL-12 p80 prior to a viral infection increases the number of resident airway macrophages, and this primes the host for a protective response against a lethal respiratory viral infection. In addition, it has been suggested that p80 functions as a competitive antagonist of IL-12 p70. Mouse Con A-activated splenocytes display identical binding affinities for p80 and IL-12, and in these cells p80 competitively inhibited IL-12 binding and IL-12-dependent proliferation. Furthermore, p80 is able to inhibit IL-12-dependent IFNγ production in freshly isolated splenocytes.
IL-12 p40 homodimer is produced by airway epithelial cells. The expression level of p40 is much higher than that of p35 in IL-12 p70-producing cells; therefore, monocytes, macrophages, neutrophils, dendritic cells, and B cells might express p40 homodimer.
p40 homodimer functions as a proinflammatory protein that enhances leukocyte accumulation in the skin, blunt Th1 immunity to Plasmodium berghei, and provides protective immunity toward mycobacterial infection. In addition, p40 homodimer induces macrophage chemotaxis independent of IL-12. Also, IL-12 p40 homodimer (p402) induces the expression of inducible nitric oxide synthase (iNOS) in microglia.
Airway epithelial cell, macrophages, microglia, and spleenocytes.
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