>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.1 EU per 1 μg of the protein by the LAL method.
36.8 kDa (p40), 22.6 kDa (p35). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Interleukin 12 (IL-12) is the founding member of the IL-12 family of heterodimeric cytokines, which have important immunological functions. IL-12 is composed of two disulfide-linked subunits of 35 kDa and 40 kDa, respectively. The 35 kDa subunit (p35) is an alpha -helical protein homologous to IL-6 and G‑CSF. The 40 kDa subunit (p40) contains one fibronectin type III and one Ig C2-like domain, and has a high degree of structural homology to type I cytokine receptors. Whereas p35 subunit is unique to IL-12, the p40 subunit is also utilized in IL-23. Mature rat p35 is a 194 amino acids (aa) protein that is secreted as a heterodimer linked to p40. It contains three potential N-linked glycosylation sites and shares 86%, and 58% aa sequence identity with mouse and human p35, respectively. Mature rat p40 contains 313 aa and can exist in multiple forms, including monomer, homodimer, heterodimer linked to p19 (forming IL-23), and heterodimer linked to p35 (forming IL-12). The expression of p40 is upregulated by substances such as LPS and CpG that activate antigen-presenting cells. Mature rat p40 shows 92% and 66% aa sequence identity to mouse and human p40, respectively. Cells known to produce IL-12 include macrophages, dendritic cells, monocytes, Langerhans cells, neutrophils, and keratinocytes. The activities of IL-12 are mediated by the receptor complex composed of two type I transmembrane proteins: a 100 kDa ligand-binding subunit (IL‑12 R beta 1) and a 130 kDa signal transducing subunit (IL‑12 R beta 2). IL‑12 facilitates hematopoietic stem cell proliferation, induces NK cell proliferation, and potentiates the expansion and late activation of Th1 CD4+ T cells (1 - 4).
Park, A.Y. and P. Scott (2001) Scand. J. Immunol. 53:529.
Trinchieri, G. et al. (2003) Immunity 19:641.
Brombacher, F. et al. (2003) Trends Immunol. 24:207.
Lankford, C.S. and D.M. Frucht (2003) J. Leukoc. Biol. 73:49.
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