Proteins

Heat Stable FGF-basic, Human is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomyocytes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Heat Stable FGF-basic, Human is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomyocytes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Heat Stable FGF-basic, Human is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomyocytes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Neuregulins or neuroregulins are a family of four structurally related proteins (NRG1, NRG2, NRG3 and NRG4) that are members of the EGF family of proteins. Studies indicate neuregulins function in nervous system development with essential roles in vertebrate embryogenesis including: cardiac development, Schwann cell and oligodendrocyte differentiation, certain aspects of neuronal development, and the formation of neuromuscular synapses. Neuregulin 1 is essential for the normal development of the nervous system and the heart. It is produced in numerous isoforms by alternative splicing, allowing it to perform a variety of functions. All NRG1 isoforms contain an EGF-like domain that is required for direct binding to ErbB3 or ErbB4 receptor tyrosine kinases. The transmembrane NRG1 isoforms contain an extracellular domain that can be proteolytically cleaved to release soluble growth factors.

Neuregulins or neuroregulins are a family of four structurally related proteins (NRG1, NRG2, NRG3 and NRG4) that are members of the EGF family of proteins. Studies indicate neuregulins function in nervous system development with essential roles in vertebrate embryogenesis including: cardiac development, Schwann cell and oligodendrocyte differentiation, certain aspects of neuronal development, and the formation of neuromuscular synapses. Neuregulin 1 is essential for the normal development of the nervous system and the heart. It is produced in numerous isoforms by alternative splicing, allowing it to perform a variety of functions. All NRG1 isoforms contain an EGF-like domain that is required for direct binding to ErbB3 or ErbB4 receptor tyrosine kinases. The transmembrane NRG1 isoforms contain an extracellular domain that can be proteolytically cleaved to release soluble growth factors.

Hepatocyte Growth Factor (HGF),also known as hepatopoietin-A and scatter factor, is a pleiotropic mitogen belonging to the peptidase S1 family (plasminogen subfamily). It is produced by mesenchymal cells and acts on epithelial cells, endothelial cells and haemopoietic progenitor cells. HGF binds to the proto-oncogenic c-Met receptor to activate a tyrosine kinase signaling cascade. It regulates cell growth, motility and morphogenesis, thus it plays a pivotal role in angiogenesis, tumorogenesis and tissue regeneration.

Hepatocyte Growth Factor (HGF),also known as hepatopoietin-A and scatter factor, is a pleiotropic mitogen belonging to the peptidase S1 family (plasminogen subfamily). It is produced by mesenchymal cells and acts on epithelial cells, endothelial cells and haemopoietic progenitor cells. HGF binds to the proto-oncogenic c-Met receptor to activate a tyrosine kinase signaling cascade. It regulates cell growth, motility and morphogenesis, thus it plays a pivotal role in angiogenesis, tumorogenesis and tissue regeneration.

Hepatocyte Growth Factor (HGF),also known as hepatopoietin-A and scatter factor, is a pleiotropic mitogen belonging to the peptidase S1 family (plasminogen subfamily). It is produced by mesenchymal cells and acts on epithelial cells, endothelial cells and haemopoietic progenitor cells. HGF binds to the proto-oncogenic c-Met receptor to activate a tyrosine kinase signaling cascade. It regulates cell growth, motility and morphogenesis, thus it plays a pivotal role in angiogenesis, tumorogenesis and tissue regeneration.

Histone H3 is one of the five main histones involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the “beads on a string” structure. Histone proteins are highly post-translationally modified however Histone H3 is the most extensively modified of the five histones. Histone H3 is an important protein in the emerging field of epigenetics, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.

Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu.4, 5 Residues 27 – 43 and 178 – 184 contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.

Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu.4, 5 Residues 27 – 43 and 178 – 184 contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.

Heregulin1-Beta1(HRG1-Beta1) is one of the isoforms encoded by Neuregulin (NRG) genes. NRGs are synthesized as large transmembrane precursor proteins, and the NRG family has 4 members and 26 isoforms. These isoforms provide large diversities, including different tissue distribution, variable potencies, and different biological functions. HRG1-β1 belongs to Type I HRG1, and is expressed in neural tissue, respiratory epithelia, and heart. In vivo, HRG1 binds and activates both ErbB3 and ErbB4, the transmembrane receptor tyrosine kinase, and is involved in the proliferation, differentiation, and survival of cells. Aberrantly produced HRG1 could be used in the constitute activation of the ErbB receptors; therefore, the upregulation of HRG1 contributes to the development of tumors, including breast cancer.

Heregulin1-Beta1(HRG1-Beta1) is one of the isoforms encoded by Neuregulin (NRG) genes. NRGs are synthesized as large transmembrane precursor proteins, and the NRG family has 4 members and 26 isoforms. These isoforms provide large diversities, including different tissue distribution, variable potencies, and different biological functions. HRG1-β1 belongs to Type I HRG1, and is expressed in neural tissue, respiratory epithelia, and heart. In vivo, HRG1 binds and activates both ErbB3 and ErbB4, the transmembrane receptor tyrosine kinase, and is involved in the proliferation, differentiation, and survival of cells. Aberrantly produced HRG1 could be used in the constitute activation of the ErbB receptors; therefore, the upregulation of HRG1 contributes to the development of tumors, including breast cancer.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

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.

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.

Inducible T-cell costimulator is an immune checkpoint protein that in humans is encoded by the ICOS gene. CD278 or ICOS (Inducible T-cell COStimulator) is a CD28-superfamily costimulatory molecule that is expressed on activated T cells. It is thought to be important for Th2 cells in particular. The protein encoded by this gene belongs to the CD28 and CTLA-4 cell-surface receptor family. It forms homodimers and plays an important role in cell-cell signaling, immune responses and regulation of cell proliferation.

Inducible T-cell costimulator is an immune checkpoint protein that in humans is encoded by the ICOS gene. CD278 or ICOS (Inducible T-cell COStimulator) is a CD28-superfamily costimulatory molecule that is expressed on activated T cells. It is thought to be important for Th2 cells in particular. The protein encoded by this gene belongs to the CD28 and CTLA-4 cell-surface receptor family. It forms homodimers and plays an important role in cell-cell signaling, immune responses and regulation of cell proliferation.

At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.

At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.

Interferon-Alpha 2a (IFN-Alpha 2a), Human produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2a shares 99.4% , 98.8% aa sequence identity with IFN-alpha 2b and 2c respectively. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2a (IFN-Alpha 2a), Human produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2a shares 99.4% , 98.8% aa sequence identity with IFN-alpha 2b and 2c respectively. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2a (IFN-Alpha 2a), Human produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2a shares 99.4% , 98.8% aa sequence identity with IFN-alpha 2b and 2c respectively. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2b (IFN-Alpha 2b) produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2b shares 99.4% aa sequence identity with both IFN-alpha 2a and 2c. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2b (IFN-Alpha 2b) produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2b shares 99.4% aa sequence identity with both IFN-alpha 2a and 2c. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2b (IFN-Alpha 2b) produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2b shares 99.4% aa sequence identity with both IFN-alpha 2a and 2c. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-beta (IFN-β), acting via STAT1 and STAT2, is known to upregulate and downregulate a wide variety of genes, most of which are involved in the antiviral immune response. It is a member of Type I IFNs, which include IFN-α, -β, τ, and –ω. IFN-β plays an important role in inducing non-specific resistance against a broad range of viral infections. It also affects cell proliferation and modulates immune responses.

Interferon-beta (IFN-β), acting via STAT1 and STAT2, is known to upregulate and downregulate a wide variety of genes, most of which are involved in the antiviral immune response. It is a member of Type I IFNs, which include IFN-α, -β, τ, and –ω. IFN-β plays an important role in inducing non-specific resistance against a broad range of viral infections. It also affects cell proliferation and modulates immune responses.

IFN-gamma Receptor II, also known as IFNGR2 and IFNGT1, is a transmembrane protein belonging to the type II cytokine receptor family. IFNGR2 is a non-ligand-binding beta chain of the IFN-gamma receptor. It is an integral part of the IFN-gamma signaling transduction pathway and is likely to interact with GAF, JAK1 and JAK2. Defects in IFNGR2 are a cause of autosomal recessive Mendelian susceptibility to mycobacterial disease (MSMD), also known as familial disseminated atypical mycobacterial infection.

IFN-gamma Receptor II, also known as IFNGR2 and IFNGT1, is a transmembrane protein belonging to the type II cytokine receptor family. IFNGR2 is a non-ligand-binding beta chain of the IFN-gamma receptor. It is an integral part of the IFN-gamma signaling transduction pathway and is likely to interact with GAF, JAK1 and JAK2. Defects in IFNGR2 are a cause of autosomal recessive Mendelian susceptibility to mycobacterial disease (MSMD), also known as familial disseminated atypical mycobacterial infection.

Human Interferon gamma (hIFN-γ) is amacrophage‐activating factor and the lone member of Interferon type II.The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Human Interferon gamma (hIFN-γ) is amacrophage‐activating factor and the lone member of Interferon type II.The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Human Interferon gamma (hIFN-γ) is amacrophage‐activating factor and the lone member of Interferon type II.The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Human Interferon gamma (hIFN-γ) is amacrophage‐activating factor and the lone member of Interferon type II.The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Human Interferon gamma (hIFN-γ) is amacrophage-activating factor and the lone member of Interferon type II. The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Human Interferon gamma (hIFN-γ) is amacrophage-activating factor and the lone member of Interferon type II. The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Human Interferon gamma (hIFN-γ) is amacrophage-activating factor and the lone member of Interferon type II. The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety 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.

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.

Interferon-gamma (IFN-γ), also known as Type II interferon or immune interferon, is a cytokine produced primarily by T-lymphocytes and natural killer cells. The protein shares no significant homology with IFN-β or the various IFN-α family proteins. Mature IFN-γ exists as noncovalently-linked homodimers. It shares high sequence indentity with mouse IFN-γ (86 %). IFN-γ was originally characterized based on its antiviral activities. The protein also exerts antiproliferative, immunoregulatory and proinflammatory activities and is thus important in host defense mechanisms. IFN-γ induces the production of cytokines, upregulates the expression of class I and II MHC antigens, Fc receptor and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching and potentiates the secretion of immunoglobulins by B cells. Additionally, IFN-γ augments TH1 cell expansion and may be required for TH1 cell differentiation.

Interferon-γ (IFN-γ), also known as Type II interferon or immune interferon, is a cytokine produced primarily by T-lymphocytes and natural killer cells. The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Interferon-γ (IFN-γ), also known as Type II interferon or immune interferon, is a cytokine produced primarily by T-lymphocytes and natural killer cells. The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

Interferon-γ (IFN-γ), also known as Type II interferon or immune interferon, is a cytokine produced primarily by T-lymphocytes and natural killer cells. The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and 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 a variety of cancers.

IL-28A, IL-28B, and IL-29, also named interferon-λ2 (IFN-λ2), IFN-λ3, and IFN-λ1, respectively, are newly identified class II cytokine receptor ligands that are distantly related to members of the IL-10 family (11-13% aa sequence identity) and the type I IFN family (15-19% aa sequence identity). The expression of IL-28A, B, and IL-29 is induced by virus infection or double-stranded RNA. All three cytokines exert bioactivities that overlap those of type I IFNs, including antiviral activity and up-regulation of MHC class I antigen expression. The three proteins signal through the same heterodimeric receptor complex that is composed of the IL-10 receptor β (IL-10 Rβ) and a novel IL-28 receptor α (IL-28 Rα, also known as IFN-λR1). Ligand binding to the receptor complex induces Jak kinase activation and STAT1 and STAT2 tyrosine phosphorylation.