1mg

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.

Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is produced by a number of different cell types, including activated T cells, B cells, macrophages, mast cells, endothelial cells, and fibroblasts, in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) is a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. On mature hematopoietic, monocytes/macrophages and eosinophils. Additionally, Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma, and adenocarcinoma cell lines.

Glia maturation factor beta (GMFB) contains an ADF-H domain，which is a member of the actin-binding proteins ADF family, GMF subfamily. It is a nerve growth factor implicated in nervous system development, angiogenesis, and immune function. GMFB causes differentiation of brain cells, stimulation of neural regeneration, and inhibition of proliferation of tumor cells. It is phosphorylated after phorbol ester stimulation and is crucial for the nervous system. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.

This product is specific for Human CD28

This product is specific for Human CD3

Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO-α, KC, neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-α). Human GRO-α, GRO-β (MIP2α),and GRO-γ (MIP2β)are products of three distinct, nonallelichuman genes. GRO-β and GRO-γ share 90% and 86% amino acid sequence homology with GROα, respectively. All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. GRO expression is inducible by serum or PDGF and/or by a variety of inflammatory mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In certain tumor cell lines, GRO is expressed constitutively. Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. Additionally, these chemokines are also active toward basophils.All three GROs can bind with high affinity to the IL-8 receptor type B.

Human GRO-α, GRO-β (MIP-2α), and GRO-γ (MIP-2β) are products of three distinct, nonallelichuman genes. GRO-β and GRO-γ share 90% and 86% amino acid sequence homology, respectively, with GROα. All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors.GRO expression is inducible by serum or PDGF and/or by a variety of inflammatory mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In certain tumor cell lines, GRO is expressed constitutively.Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils.

GRO-α/KC/CXCL1 coded by CXCL1 gene at chromosome 5 is approximately 63% identity to that of mouse MIP2. KC is also approximately 60% identical to the human GROs. Mouse KC is a potent neutrophil attractant and activator. The functional receptor for KC has been identified as CXCR2. Based on the pattern of KC expression in a number of inflammatory disease models, KC appears to have an important role in inflammation. KC was found to be involved in monocyte arrest on atherosclerotic endothelium and may also play a pathophysiological role in Alzheimer’s disease.

Guanosine-3′,5′-cyclic-monophosphothioate Sp-Isomer Sodium Salt

Heart-type fatty acid binding protein (H-FABP) is encoded by the FABP3 gene with a low molecular weight of 15 kDa. It is released in large quantities into blood at an early stage of acute myocardial infarction (AMI). H-FABP is a serum marker with high sensitivity and specificity for diagnosing AMI and myocardial ischemia.

Heart-type fatty acid binding protein (H-FABP) is encoded by the FABP3 gene with a low molecular weight of 15 kDa. It is released in large quantities into blood at an early stage of acute myocardial infarction (AMI). H-FABP is a serum marker with high sensitivity and specificity for diagnosing AMI and myocardial ischemia.

Heart-type fatty acid binding protein (H-FABP) is encoded by the FABP3 gene with a low molecular weight of 15 kDa. It is released in large quantities into blood at an early stage of acute myocardial infarction (AMI). H-FABP is a serum marker with high sensitivity and specificity for diagnosing AMI and myocardial ischemia.

Proheparin-binding EGF-like growth factor (HB-EGF), also known as DTR, DTS and HEGFL, is a member of the EGF family of mitogens. It is expressed in macrophages, monocytes, endothelial cells and muscle cells. HB-EGF signals through the EGF receptor to stimulate the proliferation of smooth muscle cells, epithelial cells and keratinocytes. Compared to EGF, HB-EGF binds to the EGF receptor with a higher affinity and has been shown to bemore mitogenic, likely due to its ability to bind to heparin and heparin sulfate proteoglycans. HB-EGF has also been reported to act as a diphtheria toxin receptor, mediating endocytosis of the bound toxin. Heparin-binding EGF-like growth factor has been shown to interact with NRD1, Zinc finger and BTB domain-containing protein 16 and BAG1.

Proheparin-binding EGF-like growth factor (HB-EGF), also known as DTR, DTS and HEGFL, is a member of the EGF family of mitogens. It is expressed in macrophages, monocytes, endothelial cells and muscle cells. HB-EGF signals through the EGF receptor to stimulate the proliferation of smooth muscle cells, epithelial cells and keratinocytes. Compared to EGF, HB-EGF binds to the EGF receptor with a higher affinity and has been shown to bemore mitogenic, likely due to its ability to bind to heparin and heparin sulfate proteoglycans. HB-EGF has also been reported to act as a diphtheria toxin receptor, mediating endocytosis of the bound toxin. Heparin-binding EGF-like growth factor has been shown to interact with NRD1, Zinc finger and BTB domain-containing protein 16 and BAG1.

Proheparin-binding EGF-like growth factor (HB-EGF), also known as DTR, DTS and HEGFL, is a member of the EGF family of mitogens. It is expressed in macrophages, monocytes, endothelial cells and muscle cells. HB-EGF signals through the EGF receptor to stimulate the proliferation of smooth muscle cells, epithelial cells and keratinocytes. Compared to EGF, HB-EGF binds to the EGF receptor with a higher affinity and has been shown to bemore mitogenic, likely due to its ability to bind to heparin and heparin sulfate proteoglycans. HB-EGF has also been reported to act as a diphtheria toxin receptor, mediating endocytosis of the bound toxin. Heparin-binding EGF-like growth factor has been shown to interact with NRD1, Zinc finger and BTB domain-containing protein 16 and BAG1.

Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of proteins. HB-EGF-like growth factor is synthesized as a membrane-anchored mitogenic and chemotactic glycoprotein. An epidermal growth factor produced by monocytes and macrophages, due to an affinity for heparin is termed HB-EGF. It has been shown to play a role in wound healing, cardiac hypertrophy and heart development and function. The transmembrane form of HB-EGF is the unique receptor for diptheria toxin and functions in juxtacrine signaling in cells. Both forms of HB-EGF participate in normal physiological processes and in pathological processes including tumor progression and metastasis, organ hyperplasia, and atherosclerotic disease. HB-EGF can bind two locations on cell surfaces, heparan sulfate proteoglycans and EGF-receptor effecting cell to cell interactions.

Glycated hemoglobin (HbA1c) is formed by hemoglobin’s exposure to plasma glucose in a non-enzymatic process. As the average amount of plasma glucose increases, the fraction of HbA1c scales up. HbA1c reflects average plasma glucose over the previous eight to twelve weeks and it can be used as a marker to measure long-term blood glucose levels. HbA1c test is routinely performed in people with type 1 and type 2 diabetes to evaluate how well diabetes is controlled. The normal range for HbA1c level is less than 6%.

Human chorionic gonadotropin (HCG) is a polypeptide hormone produced by the human placenta. HCG is a heterodimer, composed of an alpha and a beta subunit. The level of HCG is elevated in the serum of pregnant women. It is a useful marker for diagnosis of pregnancy.

Human chorionic gonadotropin (HCG) is a polypeptide hormone produced by the human placenta. HCG is a heterodimer, composed of an alpha and a beta subunit. The level of HCG is elevated in the serum of pregnant women. It is a useful marker for diagnosis of pregnancy.

Human chorionic gonadotropin (HCG) is a polypeptide hormone produced by the human placenta. HCG is a heterodimer, composed of an alpha and a beta subunit. The level of HCG is elevated in the serum of pregnant women. It is a useful marker for diagnosis of pregnancy.

Hepatitis
C virus (HCV) is a one kind of single-stranded RNA virus. It can causes liver
damage. The HCV capsid is formed by polymerization of the HCV Core Antigen (HCV
Ag). It was reported that HCV Ag could be used to diagnose active HCV infection.

Hepatitis
C virus (HCV) is a one kind of single-stranded RNA virus. It can causes liver
damage. The HCV capsid is formed by polymerization of the HCV Core Antigen (HCV
Ag). It was reported that HCV Ag could be used to diagnose active HCV infection.

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.

Glycated hemoglobin (HbA1c) is formed by hemoglobin’s exposure to plasma glucose in a non-enzymatic process. As the average amount of plasma glucose increases, the fraction of HbA1c scales up. HbA1c reflects average plasma glucose over the previous eight to twelve weeks and it can be used as a marker to measure long-term blood glucose levels. HbA1c test is routinely performed in people with type 1 and type 2 diabetes to evaluate how well diabetes is controlled. The normal range for HbA1c level is less than 6%.

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.

Human immunodeficiency virus (HIV) belongs to Lentivirus that infects humans through attacking the body’s immune system. The virus can be divided into HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV1 p24 (capsid) protein is critical in HIV-1 viral replication. HIV-1 p24 is a useful biomarker for diagnosing HIV infection.

Human immunodeficiency virus (HIV) belongs to Lentivirus that infects humans through attacking the body’s immune system. The virus can be divided into HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV1 p24 (capsid) protein is critical in HIV-1 viral replication. HIV-1 p24 is a useful biomarker for diagnosing HIV infection.

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.

Staphylococcal Protein A binds strongly and specifically to the Fc region of immunoglobulin molecules, especially IgG of many species such as Human, Rabbit, Pig, etc. The product contains five high affinity binding sites that are capable of interacting with the Fc region of IgG. HRP-Protein A is produced by covalently linking HRP to Protein A, which can be used in immuno-detection such as immunoblotting (Western or Dot blot), ELISA, and immunohistochemistry.

Protein G, a cell surface protein of Group G streptococci, is a Type III Fc receptor that binds to the Fc region of IgG by a non-immune mechanism similar to that of protein A. It contains 3 IgG binding domains and is engineered to delete albumin-binding region. HRP has been covalently coupled to Protein G to produce the HRP-Protein G, which can be used in detection systems such as immunoblotting, ELISA, immunoperoxidase electron microscopy and immunohistochemistry.

Protein L is a cell surface protein expressed by Peptostreptoccocus magnus, that binds to the variable light chains (kappa chains) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins such as protein A and protein G, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. HRP-Protein L is produced by covalently linking HRP to protein L. The complex can be used in immuno-detection such as immunoblotting (western or dot blot), ELISA, and immunohistochemistry.

C-reactive protein (CRP) is synthesized in the liver by macrophage. Its level in blood increases when inflammation occurs. CRP serves as a useful marker for diagnosis of inflammation. High-sensitivity C-reactive protein (hsCRP), can serve as a risk marker for the diagnosis of myocardial infarction, ischemic stroke, peripheral vascular disease. Measuring hsCRP in blood is helpful to provide positive treatment of the disease.

C-reactive protein (CRP) is synthesized in the liver by macrophage. Its level in blood increases when inflammation occurs. CRP serves as a useful marker for diagnosis of inflammation. High-sensitivity C-reactive protein (hsCRP), can serve as a risk marker for the diagnosis of myocardial infarction, ischemic stroke, peripheral vascular disease. Measuring hsCRP in blood is helpful to provide positive treatment of the disease.

IgE is a type of immunoglobulins produced by the immune system. It is composed of two heavy chains and two light chains, like Ig molecules. IgE plays an essential role in various allergic reactions. Its main function is immunity to parasites such as Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica. It also plays an important role in type I hypersensitivity. Total IgE is considered as a significant marker of allergic state.

IgE is a type of immunoglobulins produced by the immune system. It is composed of two heavy chains and two light chains, like Ig molecules. IgE plays an essential role in various allergic reactions. Its main function is immunity to parasites such as Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica. It also plays an important role in type I hypersensitivity. Total IgE is considered as a significant marker of allergic state.

Immunoglobulins (Ig) and free light chains (FLC) is involved in humoral immune response. Ig is composed of two identical light chains and two identical heavy chains. FLC contains two types: kappa free light chain (KFLC) and lambda free light chain (LFLC). The expression of Kappa or Lambda is greatly increased in multiple myeloma or other B cell malignancies. It is useful for the identification of certain non-Hodgkin’s lymphomas, leukemias and plasmacytomas. Immunohistochemistry is commonly applied for the detection of free light chains.

Immunoglobulins (Ig) and free light chains (FLC) is involved in humoral immune response. Ig is composed of two identical light chains and two identical heavy chains. FLC contains two types: kappa free light chain (KFLC) and lambda free light chain (LFLC). The expression of Kappa or Lambda is greatly increased in multiple myeloma or other B cell malignancies. It is useful for the identification of certain non-Hodgkin’s lymphomas, leukemias and plasmacytomas. Immunohistochemistry is commonly applied for the detection of free light chains.

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.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

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.

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.

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.

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.