Rat IL-12 Antibody

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). 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 beta1) and a 130 kDa signal transducing subunit (IL‑12 R beta2). 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).