IL-23 Protein, Human (Biotinylated, HEK293, His)

IL-23, in collaboration with IL12B, forms the pro-inflammatory cytokine IL-23, playing diverse roles in both innate and adaptive immunity. Released by antigen-presenting cells such as dendritic cells or macrophages, IL-23 binds to a heterodimeric receptor complex comprising IL12RB1 and IL23R, initiating a cascade involving JAK2 and TYK2 activation. These kinases phosphorylate the receptor, creating a docking site for the subsequent phosphorylation of STAT3 and STAT4. This process activates multiple pathways, including p38 MAPK or NF-kappa-B, fostering the production of pro-inflammatory cytokines, such as interleukin-17A/IL17A. Additionally, IL-23 actively participates in the early and effective clearance of intracellular bacteria. Notably, IL-23 promotes the expansion and survival of T-helper 17 cells, a CD4-positive helper T-cell subset known for producing IL-17, alongside other IL-17-producing cells. The heterodimeric association of IL-23 with IL12B, known as interleukin IL-23, is disulfide-linked. Furthermore, IL-23 interacts with IL23R, facilitating the recruitment of IL12RB1.