Cytokines & Chemokines

Interleukin-12 (IL-12), also known as NKSF, TCMF, CLMF and TSF, is a heterodimeric cytokine composed of p35 and p40 subunits. It is produced by monocytes, macrophages, B cells and dendritic cells in response to bacterial lipopolysaccharides and intracellular pathogens. IL-12 signals throughtheIL-12 receptor complex, which is comprised of IL-12 Rβ1 and IL-12 Rβ2. IL-12 induces the proliferation and activation of hematopoietic stem cells, natural killer cells and T- cells. It is indispensible during the development of Th1 cells, leading to the production of IFN-gamma and IL-2.

Interleukin-12 (IL-12), also known as NKSF, TCMF, CLMF and TSF, is a heterodimeric cytokine composed of p35 and p40 subunits. It is produced by monocytes, macrophages, B cells and dendritic cells in response to bacterial lipopolysaccharides and intracellular pathogens. IL-12 signals throughtheIL-12 receptor complex, which is comprised of IL-12 Rβ1 and IL-12 Rβ2. IL-12 induces the proliferation and activation of hematopoietic stem cells, natural killer cells and T- cells. It is indispensible during the development of Th1 cells, leading to the production of IFN-gamma and IL-2.

Interleukin-12 (IL-12), also known as NKSF, TCMF, CLMF and TSF, is a heterodimeric cytokine composed of p35 and p40 subunits. It is produced by monocytes, macrophages, B cells and dendritic cells in response to bacterial lipopolysaccharides and intracellular pathogens. IL-12 signals throughtheIL-12 receptor complex, which is comprised of IL-12 Rβ1 and IL-12 Rβ2. IL-12 induces the proliferation and activation of hematopoietic stem cells, natural killer cells and T- cells. It is indispensible during the development of Th1 cells, leading to the production of IFN-gamma and IL-2.

Noggin, also known as NOG, is a homodimeric glycoprotein that bindsto and modulates the activity of TGF-beta family ligands. It is expressed in condensing cartilage and immature chondrocytes. Noggin antagonizes bone morphogenetic protein (BMP) activities by blocking epitopes on BMPs needed for binding to their receptors. Noggin has been shown to be involved in many developmental processes, such as neural tube formation and joint formation. During development, Noggin diffuses through extracellular matrices and forms morphogenic gradients, regulating cellular responses dependent on the local concentration of the signaling molecule.

Noggin, also known as NOG, is a homodimeric glycoprotein that bindsto and modulates the activity of TGF-beta family ligands. It is expressed in condensing cartilage and immature chondrocytes. Noggin antagonizes bone morphogenetic protein (BMP) activities by blocking epitopes on BMPs needed for binding to their receptors. Noggin has been shown to be involved in many developmental processes, such as neural tube formation and joint formation. During development, Noggin diffuses through extracellular matrices and forms morphogenic gradients, regulating cellular responses dependent on the local concentration of the signaling molecule.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Herpes Virus Entry Mediator (HVEM) is a transmembrane protein that is the receptor for TNFSF14 (also known as LIGHT) and is therefore referred to asTNFRSF14. HVEM is expressed broadly on immune cells such as T cells, natural killer (NK) cells and monocytes. The interaction of 3 molecules of LIGHT with three molecules of HVEM forms a hexameric complex that leads to the recruitment and retention of effector cells and activates NK cells to produce large amounts of IFN-γ and GM-CSF. In addition to the canonical binding partner LIGHT, HVEM can also bind to the inhibitory signaling protein, B- and T- lymphocyte attenuator (BTLA), which suppresses immune responses. Therefore, the HVEM network plays an important role in regulating immunity and the behavior of lymphocytes.