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.
Interleukin 12 receptor; beta 1 is also known as IL-12 receptor beta component; IL-12R subunit beta-1; and CD212 antigen (CD212). IL12RB1(CD212) is a subunit of the interleukin 12 receptor. IL12RB1(CD212) is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. This protein binds to interleukine 12 (IL12) with a low affinity; and is thought to be a part of IL12 receptor complex. IL12RB1(CD212) forms a disulfide-linked oligomer; which is required for its IL12 binding activity. The coexpression of IL12RB1 and IL12RB2 proteins was shown to lead to the formation of high-affinity IL12 binding sites and reconstitution of IL12 dependent signaling. The lack of expression of this gene was found to result in the immunodeficiency of patients with severe mycobacterial and Salmonella infections. IL12RB1(CD212) Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. It associated with IL12RB2 it forms a functional; high affinity receptor for IL12. IL12RB1(CD212) associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade.
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.
Interleukin 13 (IL-13) is a single-chain glycosylated polypeptide, which belongs to the IL-13/IL-4 family. IL-13 protein is secreted by many cell types, but especially by T helper type 2 (Th2) cells. IL-13 exerts its effects through a multi-subunit receptor comprising the alpha chain of the IL-4 receptor (IL-4R&alpha,) and at least one of two known IL-13-specific binding chains (IL-13 R&alpha,1 and IL-13 R&alpha,2). As a cytokine, IL-13 protein is critical in regulating inflammatory, immune responses and diseases. In addition, it inhibits the production of pro-inflammatory cytokines and chemokines, and thus down-regulates macrophage activity. IL-13 protein and antibody is more importantly implicated as a central mediator of immunoregulatory processes in various cell types.
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