Interleukin-12 subunit beta (IL-12B) belongs to the type I cytokine receptor family. It contains 1 fibronectin type-III domain and 1 Ig-like C2-type domain. IL-12B is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. IL-12 is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor encoded by IL12B and a 35 kD subunit encoded by IL12A. IL12 is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. It has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen.
Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC.
Interleukin12 receptor subunit beta 1 (IL12RB1) is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. IL12RB1 can spontaneously form homodimers and -oligomers; which are able to bind IL12 with only low affinity. IL12 high affinity receptor complex is composed of two subunits designated IL12RB1 and IL12RB2. While IL12RB1 interacts with the IL-12p40 subunit; IL-12p35 is mainly connecting with IL12RB2. This receptor chain is also responsible for transmitting the IL12 signal into the cell. IL12RB1; to the contrary; is also part of the IL23R; where it interacts with the p40 subunit of IL23. IL12RB1 is expressed in activated T cells; NK cells and B cells.
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