Cytokines & Chemokines

Sharing 41% sequence identity with human Interferon gamma (hIFN--γ), mouse IFN gamma (mIFN--γ)is a macrophage-activating factor.The active form of IFN--γ is an antiparallel dimer that sets off IFN--γ/JAK/STAT pathway. IFN--γ signaling does diverse biological functions primarily related to host defense and immune regulation, including antiviral and antibacterial defense, apoptosis, inflammation, and innate and acquired immunity.While IFN--γ–induced inflammatory cascade summons a variety of immune-related cell types, such as macrophages, natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), IFN--γ is also implicated in resistance to NK cell and CTL responses and in immune escape in avariety of cancers.

Sharing 41% sequence identity with human Interferon gamma (hIFN--γ), mouse IFN gamma (mIFN--γ)is a macrophage-activating factor.The active form of IFN--γ is an antiparallel dimer that sets off IFN--γ/JAK/STAT pathway. IFN--γ signaling does diverse biological functions primarily related to host defense and immune regulation, including antiviral and antibacterial defense, apoptosis, inflammation, and innate and acquired immunity.While IFN--γ–induced inflammatory cascade summons a variety of immune-related cell types, such as macrophages, natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), IFN--γ is also implicated in resistance to NK cell and CTL responses and in immune escape in avariety of cancers.

Sharing 41% sequence identity with human Interferon gamma (hIFN--γ), mouse IFN gamma (mIFN--γ)is a macrophage-activating factor.The active form of IFN--γ is an antiparallel dimer that sets off IFN--γ/JAK/STAT pathway. IFN--γ signaling does diverse biological functions primarily related to host defense and immune regulation, including antiviral and antibacterial defense, apoptosis, inflammation, and innate and acquired immunity.While IFN--γ–induced inflammatory cascade summons a variety of immune-related cell types, such as macrophages, natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), IFN--γ is also implicated in resistance to NK cell and CTL responses and in immune escape in avariety of cancers.

Sharing 41% sequence identity with human Interferon gamma (hIFN--γ), mouse IFN gamma (mIFN--γ)is a macrophage-activating factor.The active form of IFN--γ is an antiparallel dimer that sets off IFN--γ/JAK/STAT pathway. IFN--γ signaling does diverse biological functions primarily related to host defense and immune regulation, including antiviral and antibacterial defense, apoptosis, inflammation, and innate and acquired immunity.While IFN--γ–induced inflammatory cascade summons a variety of immune-related cell types, such as macrophages, natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), IFN--γ is also implicated in resistance to NK cell and CTL responses and in immune escape in avariety of cancers.

Tumor necrosis factor alpha (TNF-α) is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. Mouse TNF-α occurs as a membrane-anchored form. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. The biologically active native form of TNF-α is reportedly a trimer. Human and mouse TNF-α show approximately 79% homology at the amino acid level and crossreactivity between the two species.

Tumor necrosis factor alpha (TNF-α) is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. Mouse TNF-α occurs as a membrane-anchored form. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. The biologically active native form of TNF-α is reportedly a trimer. Human and mouse TNF-α show approximately 79% homology at the amino acid level and crossreactivity between the two species.

Tumor necrosis factor alpha (TNF-α) is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. Mouse TNF-α occurs as a membrane-anchored form. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. The biologically active native form of TNF-α is reportedly a trimer. Human and mouse TNF-α show approximately 79% homology at the amino acid level and crossreactivity between the two species.

Fibroblast Growth Factor- acidic (FGF-acidic), also known as FGF-1 and endothelial cell growth factor, is a member of the FGF family which currently contain 23 members. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF acidic has been detected in large amounts in the brain. Other cells known to express FGF acidic include hepatocytes, vascular smooth muscle cells, CNS neurons, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelium cells and pituitary basophils and acidophils. As with other FGF's, FGF acidic exhibits considerable species cross reactivity. FGF acidic and FGF basic stimulate the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin.

Fibroblast Growth Factor- acidic (FGF-acidic), also known as FGF-1 and endothelial cell growth factor, is a member of the FGF family which currently contain 23 members. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF acidic has been detected in large amounts in the brain. Other cells known to express FGF acidic include hepatocytes, vascular smooth muscle cells, CNS neurons, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelium cells and pituitary basophils and acidophils. As with other FGF's, FGF acidic exhibits considerable species cross reactivity. FGF acidic and FGF basic stimulate the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin.