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Human IL-31 is a T-cell derived cytokine that shares several structural and functional characteristics with IL-6, Oncostatin M, LIF, and Cardiotrophin-1. It signals through a receptor complex comprised of GPL (GP130-like, IL-31RA) and OSMR (Oncostatin M receptor). GPL/OSMR signaling is a strong activator of STAT3 and STAT5, and can also activate STAT1, Jak1, and Jak2 signaling pathways. IL-31 regulated immune responses have been implicated in skin physiology and inflammatory skin diseases.

Human IL-31 is a T-cell derived cytokine that shares several structural and functional characteristics with IL-6, Oncostatin M, LIF, and Cardiotrophin-1. It signals through a receptor complex comprised of GPL (GP130-like, IL-31RA) and OSMR (Oncostatin M receptor). GPL/OSMR signaling is a strong activator of STAT3 and STAT5, and can also activate STAT1, Jak1, and Jak2 signaling pathways. IL-31 regulated immune responses have been implicated in skin physiology and inflammatory skin diseases.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

Interleukin-33 (IL-33) is a proinflammatory cytokine that belongs to the IL-1 family. IL-33 is expressed in a variety of cells, including epithelial and endothelial cells, smooth muscle cells, macrophages and fibroblasts. The primary receptors for IL-33 are ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which belong to the IL-1 receptor family. IL-33 is localized to the nucleus of resting cells where it binds to chromatin in the H2A-H2B histone complex as a transcriptional suppressor. IL-33 is secreted by cells during injury which induces a T-helper 2 type inflammatory response. Evidence suggests IL-33 plays a role in autoimmune disease. IL-33’s interaction with ST2 can drive allergic pathology and IL-33 has been reported to play a role in the development of rheumatoid arthritis and systemic lupus erythematosus.

Monoclonal Antibodies

Monoclonal Antibodies

Interleukin-4 Receptor, also known as IL-4RA and CD124, is a transmembrane glycoprotein belonging to the class I receptor family. It is highly expressed by activated T-cells. IL-4RA couples with γ chain to form the type I receptor for IL-4. The extracellular domain of IL-4RA binds to IL-4 and antagonizes its activity. IL-4RA plays an important role in Th2 cell differentiation, Ig class switching and alternative macrophage activation. It has also been implicated in allergic inflammation, tumor progression and atherogenesis.

Interleukin-4 Receptor, also known as IL-4RA and CD124, is a transmembrane glycoprotein belonging to the class I receptor family. It is highly expressed by activated T-cells. IL-4RA couples with γ chain to form the type I receptor for IL-4. The extracellular domain of IL-4RA binds to IL-4 and antagonizes its activity. IL-4RA plays an important role in Th2 cell differentiation, Ig class switching and alternative macrophage activation. It has also been implicated in allergic inflammation, tumor progression and atherogenesis.

Interleukin-4 Receptor, also known as IL-4RA and CD124, is a transmembrane glycoprotein belonging to the class I receptor family. It is highly expressed by activated T-cells. IL-4RA couples with γ chain to form the type I receptor for IL-4. The extracellular domain of IL-4RA binds to IL-4 and antagonizes its activity. IL-4RA plays an important role in Th2 cell differentiation, Ig class switching and alternative macrophage activation. It has also been implicated in allergic inflammation, tumor progression and atherogenesis.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4+ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4+ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, mediates the activities of eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, mediates the activities of eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, mediates the activities of eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.

Interleukin-5 Receptor alpha (IL-5Rα, CD125) is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology. Mature human IL-5 Rα consists of a 322 aa extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain. Within the ECD, human IL-5Rα shares 71% aa sequence identity with mouse and rat IL-5 Rα. Alternate splicing of human IL-5 Rα generates soluble secreted forms which function as IL-5 antagonists. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Rα and the transmembrane common β chain (βc/CD131) which is shared with the receptor complexes for IL-3 and GMCSF. IL-5 Rα binds IL-5 at low affinity and then associates with preformed βc oligomers to form the signaling competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5Rα followed by eosinophilic differentiation and activation.

Interleukin-5 Receptor alpha (IL-5Rα, CD125) is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology. Mature human IL-5 Rα consists of a 322 aa extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain. Within the ECD, human IL-5Rα shares 71% aa sequence identity with mouse and rat IL-5 Rα. Alternate splicing of human IL-5 Rα generates soluble secreted forms which function as IL-5 antagonists. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Rα and the transmembrane common β chain (βc/CD131) which is shared with the receptor complexes for IL-3 and GMCSF. IL-5 Rα binds IL-5 at low affinity and then associates with preformed βc oligomers to form the signaling competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5Rα followed by eosinophilic differentiation and activation.

Interleukin-5 Receptor alpha (IL-5Rα, CD125) is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology. Mature human IL-5 Rα consists of a 322 aa extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain. Within the ECD, human IL-5Rα shares 71% aa sequence identity with mouse and rat IL-5 Rα. Alternate splicing of human IL-5 Rα generates soluble secreted forms which function as IL-5 antagonists. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Rα and the transmembrane common β chain (βc/CD131) which is shared with the receptor complexes for IL-3 and GMCSF. IL-5 Rα binds IL-5 at low affinity and then associates with preformed βc oligomers to form the signaling competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5Rα followed by eosinophilic differentiation and activation.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that participates in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, and nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction and released into the blood stream to help break down fats and improve insulin resistance.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that participates in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, and nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction and released into the blood stream to help break down fats and improve insulin resistance.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that participates in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, and nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction and released into the blood stream to help break down fats and improve insulin resistance.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that participates in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, and nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction and released into the blood stream to help break down fats and improve insulin resistance.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that participates in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, and nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction and released into the blood stream to help break down fats and improve insulin resistance.

Interleukin-6 (IL-6), also known as BSF-2, CDF and IFNB2, is a pleiotropic cytokine that acts in both pro-inflammatory and anti-inflammatory responses. It is produced mainly by T cells, macrophages, monocytes, endothelial cells and muscle cells. IL-6 binds to IL-6 receptor (IL-6R) to trigger the association of IL-6R with gp130, inducing signal transduction through JAKs and STATs. The biological functions of IL-6 are diverse. It stimulates B cell differentiation and antibody production, myeloma and plasmacytoma growth, as well as nerve cell differentiation. It also acts as a myokine, produced by muscle cells in response to muscle contraction, to be released to the blood stream to help break down fats and improve insulin resistance.