Animal-Free IL-12 alpha Protein, Mouse (His)

The IL-12 alpha Protein is capable of heterodimerizing with IL12B to form the IL-12 cytokine or with EBI3/IL27B to form the IL-35 cytokine. IL-12 is predominantly produced by professional antigen-presenting cells such as B-cells, dendritic cells, macrophages, and granulocytes. It plays a crucial role in regulating T-cell and natural killer-cell responses, inducing interferon-gamma (IFN-gamma) production, promoting the differentiation of T-helper 1 (Th1) cells, and bridging innate resistance with adaptive immunity. The IL-12 receptor, composed of IL12R1 and IL12R2 subunits, mediates the biological effects of IL-12 by initiating the tyrosine phosphorylation of cellular substrates, including TYK2 and JAK2 kinases. The recruited phosphorylated STAT4 translocates to the nucleus, where it regulates the expression of cytokine and growth factor responsive genes. As part of IL-35, IL-12 alpha Protein plays vital roles in maintaining immune homeostasis in the liver microenvironment and serves as an immune-suppressive cytokine. Signaling occurs through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers, requiring the involvement of transcription factors STAT1 and STAT4. The formation of a unique heterodimer between STAT1 and STAT4 enables binding to specific DNA sites. The IL-12 alpha Protein can form disulfide-linked heterodimers with IL12B, known as interleukin IL-12, and non-disulfide-linked heterodimers with EBI3/IL27B, known as interleukin IL-35. Additionally, it interacts with NBR1, promoting IL-12 secretion.