IL-12 Protein, Rat (HEK293, His)

The IL-12 Protein has the ability to heterodimerize with IL12B to form the IL-12 cytokine, or with EBI3/IL27B to form the IL-35 cytokine. It is primarily produced by professional antigen-presenting cells such as B-cells, dendritic cells, macrophages, and granulocytes, and plays a crucial role in regulating T-cell and natural killer-cell responses. IL-12 stimulates the production of interferon-gamma and promotes the differentiation of T-helper 1 cells, bridging the gap between innate resistance and adaptive immunity. Its biological effects are mediated through a receptor composed of IL12R1 and IL12R2 subunits, leading to the phosphorylation of cellular substrates including TYK2 and JAK2. This, in turn, activates STAT4 and facilitates the regulation of cytokine/growth factor responsive genes. In the context of IL-35, IL-12 Protein contributes to maintaining immune homeostasis in the liver microenvironment and acts as an immune-suppressive cytokine. Its signaling occurs through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers, and requires the involvement of transcription factors STAT1 and STAT4. Furthermore, IL-12 Protein can form a disulfide-linked heterodimer with IL12B, known as interleukin IL-12, and a non-disulfide-linked heterodimer with EBI3/IL27B, known as interleukin IL-35. Additionally, it interacts with NBR1, promoting the secretion of IL-12.