Cytokines & Chemokines

Interleukin-6 Receptor Alpha, also known as IL-6RA, IL-6R1 and CD126, belongs to the type I cytokine receptor family. It is mainly expressed on T cells, fibroblasts and macrophages. IL-6RA couples with gp130 to form the IL-6 receptor; IL-6RA binds specifically to IL-6 and depends on gp130 to transmit signals. IL-6RA dysfunction has been correlated with the pathogenesis of many diseases, such as multiple myeloma, autoimmune diseases and prostate cancer. Soluble IL-6RA, which consists of only the extracellular domain of IL-6RA, acts as an agonist of IL-6 activity.

Interleukin-6 Receptor Alpha, also known as IL-6RA, IL-6R1 and CD126, belongs to the type I cytokine receptor family. It is mainly expressed on T cells, fibroblasts and macrophages. IL-6RA couples with gp130 to form the IL-6 receptor; IL-6RA binds specifically to IL-6 and depends on gp130 to transmit signals. IL-6RA dysfunction has been correlated with the pathogenesis of many diseases, such as multiple myeloma, autoimmune diseases and prostate cancer. Soluble IL-6RA, which consists of only the extracellular domain of IL-6RA, acts as an agonist of IL-6 activity.

Interleukin-8 (IL-8), also known as CXCL8, GCP-1 and NAP-1, is one of the first discovered chemokines and belongs to the CXCL family, in which the first two conserved cysteines are separated by one residue. In vivo, IL-8 exists in two forms: a 77 a.a. protein produced by endothelial cells, and the more active 72 a.a. protein produced by monocytes. The receptors for IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. The functions of IL-8 are to induce rapid changes in cell morphology, activate integrins, and release the granule contents of neutrophils. Thus, IL-8 can enhance the antimicrobial actions of defense cells. It is secreted by monocytes, macrophages and endothelial cells. IL-8 signals through CXCR1 and CXCR2 to chemoattract neutrophils, basophils, and T cells. IL-8 is also a potent promoter of angiogenesis. Other functions of this protein, such as involvement in bronchiolitis pathogenesis, have also been reported.

Interleukin-8 (IL-8), also known as CXCL8, GCP-1 and NAP-1, is one of the first discovered chemokines and belongs to the CXCL family, in which the first two conserved cysteines are separated by one residue. In vivo, IL-8 exists in two forms: a 77 a.a. protein produced by endothelial cells, and the more active 72 a.a. protein produced by monocytes. The receptors for IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. The functions of IL-8 are to induce rapid changes in cell morphology, activate integrins, and release the granule contents of neutrophils. Thus, IL-8 can enhance the antimicrobial actions of defense cells. It is secreted by monocytes, macrophages and endothelial cells. IL-8 signals through CXCR1 and CXCR2 to chemoattract neutrophils, basophils, and T cells. IL-8 is also a potent promoter of angiogenesis. Other functions of this protein, such as involvement in bronchiolitis pathogenesis, have also been reported.

Interleukin-8 (IL-8), also known as CXCL8, GCP-1 and NAP-1, is one of the first discovered chemokines and belongs to the CXCL family, in which the first two conserved cysteines are separated by one residue. In vivo, IL-8 exists in two forms: a 77 a.a. protein produced by endothelial cells, and the more active 72 a.a. protein produced by monocytes. The receptors for IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. The functions of IL-8 are to induce rapid changes in cell morphology, activate integrins, and release the granule contents of neutrophils. Thus, IL-8 can enhance the antimicrobial actions of defense cells. It is secreted by monocytes, macrophages and endothelial cells. IL-8 signals through CXCR1 and CXCR2 to chemoattract neutrophils, basophils, and T cells. IL-8 is also a potent promoter of angiogenesis. Other functions of this protein, such as involvement in bronchiolitis pathogenesis, have also been reported.

Ciliary Neurotrophic Factor (CNTF) is a cytokine belonging to the Interleukin 6 (IL-6) family, which also includes IL-6, Oncostatin M, Leukemia Inhibitory Factor (LIF), and Cardiotrophin-1. Structurally, CNTF resembles a four-helix bundle composition, similar to the other members of the IL-6 family. The receptor for CNTF is composed of three parts: a gp130-like subunit common in the IL-6 receptor family, a LIF Receptor β subunit, and a CNTF specific α receptor subunit. Upon binding to the CNTF, the β subunit of the CNTF receptor will undergo tyrosine phosphorylation, and activate the intracellular JAK/STAT pathway. The main function of CNTF in vivo is to promote the differentiation and survival of a variety of neurons and glial cells, including sympathetic precursor cells and spinal motor neurons.

Ciliary Neurotrophic Factor (CNTF) is a cytokine belonging to the Interleukin 6 (IL-6) family, which also includes IL-6, Oncostatin M, Leukemia Inhibitory Factor (LIF), and Cardiotrophin-1. Structurally, CNTF resembles a four-helix bundle composition, similar to the other members of the IL-6 family. The receptor for CNTF is composed of three parts: a gp130-like subunit common in the IL-6 receptor family, a LIF Receptor β subunit, and a CNTF specific α receptor subunit. Upon binding to the CNTF, the β subunit of the CNTF receptor will undergo tyrosine phosphorylation, and activate the intracellular JAK/STAT pathway. The main function of CNTF in vivo is to promote the differentiation and survival of a variety of neurons and glial cells, including sympathetic precursor cells and spinal motor neurons.

Ciliary Neurotrophic Factor (CNTF) is a cytokine belonging to the Interleukin 6 (IL-6) family, which also includes IL-6, Oncostatin M, Leukemia Inhibitory Factor (LIF), and Cardiotrophin-1. Structurally, CNTF resembles a four-helix bundle composition, similar to the other members of the IL-6 family. The receptor for CNTF is composed of three parts: a gp130-like subunit common in the IL-6 receptor family, a LIF Receptor β subunit, and a CNTF specific α receptor subunit. Upon binding to the CNTF, the β subunit of the CNTF receptor will undergo tyrosine phosphorylation, and activate the intracellular JAK/STAT pathway. The main function of CNTF in vivo is to promote the differentiation and survival of a variety of neurons and glial cells, including sympathetic precursor cells and spinal motor neurons.

VEGF-A121 is one of five isoforms (121, 145, 165, 189, and 206) of VEGF protein, a cytokine belonging to the Platelet Differentiation Growth Factor (PDGF) family, and existing as a disulfide-linked homodimeric glycoprotein. In contrast to the longer isoforms, VEGF-A121 is more freely diffusible, and cannot bind to heparin. In vivo, VEGF is expressed predominantly in lung, heart, kidney, and adrenal glands, and the expression of VEGF is up-regulated by a number of growth factors, including PDGF, Fibroblast Growth Factor (FGF), Epidermal Growth Factor (EGF), and Tumor Necrosis Factor (TNF). VEGF signals via binding to two tyrosine kinase receptors: the Fms-like tyrosine kinase 1 (Flt-1) and the kinase domain receptor (KDR). VEGF is a specific mitogen and survival factor, contributing to abnormal angiogenesis and cancer development.