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

IL-35 Protein plays a pivotal role in immune regulation, exhibiting versatility in its functions. It heterodimerizes with IL12B to form the IL-12 cytokine or with EBI3/IL27B to create the IL-35 cytokine. IL-12, primarily produced by professional antigen-presenting cells such as B-cells, dendritic cells, macrophages, and granulocytes, serves as a crucial link between innate resistance and adaptive immunity, regulating T-cell and natural killer-cell responses while inducing interferon-gamma production and favoring the differentiation of T-helper 1 cells. Mechanistically, IL-12 exerts its effects through a receptor composed of IL12R1 and IL12R2 subunits, leading to tyrosine phosphorylation of cellular substrates and subsequent regulation of cytokine/growth factor responsive genes by recruited phosphorylated STAT4. In the context of IL-35, IL-35 contributes significantly to maintaining immune homeostasis in the liver microenvironment and functions as an immune-suppressive cytokine. Notably, IL-35 mediates its effects through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers, requiring the transcription factors STAT1 and STAT4 for signaling. Additionally, IL-35 interacts with NBR1, promoting IL-12 secretion. The IL-35 heterodimer with EBI3/IL27B, known as interleukin IL-35, is not disulfide-linked, distinguishing it from the disulfide-linked IL-12 heterodimer with IL12B.