Cytokines

Colony Stimulating Factor 1 (CSF1), previously called Macrophage Colony Stimulating Factor (M-CSF), is a hematopoietic growth factor that is involved in the proliferation, differentiation, and survival of monocytes, macrophages, and bone marrow progenitor cells. It is produced by osteoblasts (as a result of endocrine stimulation by parathyroid hormone), exerts paracrine effects on osteoclasts and can interact with CSF1R. CSF1 is a four α-helical bundle cytokine and its active form is found extracellularly as a disulfide-linked homodimer. Four transcript variants encoding three different isoforms have been reported for CSF1 gene. Although forms may vary, all of them contain the N-terminal 150 amino acid portion that is necessary and sufficient for interaction with the receptor. The first 223 amino acid of mature human CSF1 shares 88%, 86%, 81% and 74% sequence identity with corresponding regions of dog, cow, mouse and rat CSF1, respectively. Human CSF1 is active in the mouse, but mouse CSF1 is reported to be species-specific.

Recombinant Murine Colony Stimulating Factor 1 (Macrophage) (CSF1), formerly called Macrophage Colony Stimulating Factor (M-CSF), is a hematopoietic growth factor that is involved in the proliferation, differentiation, and survival of monocytes, macrophages, and bone marrow progenitor cells. It is produced by osteoblasts (as a result of endocrine stimulation by parathyroid hormone) exerts paracrine effects on osteoclasts and can interact with CSF1R. CSF1 is a four α-helical bundle cytokine and its active form is found extracellularly as a disulfide-linked homodimer. Four transcript variants encoding three different isoforms have been reported for CSF1 gene. Although forms may vary, all of them contain the N-terminal 150 amino acid portion that is necessary and sufficient for interaction with the receptor. The first 229 amino acids of mature mouse CSF1 shares 87%, 83%, 82% and 81% sequence identity with corresponding regions of rat, dog, cow and human CSF1, respectively. Human CSF1 is active in the mouse, but mouse CSF1 is reported to be species-specific.

Colony Stimulating Factor 2 (CSF2), previously called Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF), is secreted by a number of different cell types (including activated T cells, B cells, macrophages, mast cells, endothelial cells and fibroblasts) in response to cytokine or immune and inflammatory stimulation. It was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors and has functions of stimulates the growth and differentiation of hematopoietic precursor cells from various lineages. CSF2 has also been reported to have a functional role on non-hematopoietic cells and can induce human endothelial cells to migrate and proliferate. Additionally, it can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines. It is reported that CSF2 has no biological effects across species.

Colony Stimulating Factor 2 (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It 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 or immune and inflammatory stimuli. CSF2 is also a growth factor for erythroid, megakaryocyte and eosinophil progenitors. On mature hematopoietic cells, CSF2 is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages and eosinophils. It can induce human endothelial cells to migrate and proliferate and can also stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines. CSF2 is species specific and human CSF2 has no biological effects on mouse cells.

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GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

Recombinant Murine Colony Stimulating Factor 2 (granulocyte-macrophage)
CSF2
GM-CSF, GMCSF
Molgramostin
MGI-1GM (Macrophage granulocyte inducer-1GM)

Colony Stimulating Factor 2 (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It 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 or immune and inflammatory stimuli. On mature hematopoietic cells, CSF2 is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages and eosinophils. CSF2 promotes a Th1 biased immune response, angiogenesis, allergic inflammation and the development of autoimmunity. It shows clinical effectiveness in ameliorating chemotherapy-induced neutropenia, and CSF2 transfected tumor cells are utilized as cancer vaccines. Mature mouse CSF2 shares 49% - 54% amino acid sequence identity with canine, feline, human, and porcine CSF2 and 69% with rat CSF2. The activity of CSF2 is species specific between human and mouse. Mouse CSF2 is only weakly active on rat cells, although rat CSF2 is fully active on mouse cells.

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Source: Escherichia coli

Colony Stimulating Factor 2 (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It 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 or immune and inflammatory stimuli. On mature hematopoietic cells, CSF2 is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages and eosinophils. CSF2 promotes a Th1 biased immune response, angiogenesis, allergic inflammation and the development of autoimmunity. It shows clinical effectiveness in ameliorating chemotherapy-induced neutropenia, and CSF2 transfected tumor cells are utilized as cancer vaccines. Mature rat CSF2 shares 69% with mouse CSF2. Rat CSF2 is fully active on mouse cells, although Mouse CSF2 is only weakly active on rat cells.

Colony Stimulating Factor 2 (CSF2), previously called Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF), is secreted by a number of different cell types (including activated T cells, B cells, macrophages, mast cells, endothelial cells and fibroblasts) in response to cytokine or immune and inflammatory stimulation. It was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors and has functions of stimulates the growth and differentiation of hematopoietic precursor cells from various lineages. CSF2 has also been reported to have a functional role on non-hematopoietic cells and can induce human endothelial cells to migrate and proliferate. Additionally, it can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines. It is reported that CSF2 has no biological effects across species.

Colony Stimulating Factor 3 (G-CSF) is a pleiotropic cytokine best known for its specific effects on the proliferation, differentiation and activation of hematopoietic cells of the neutrophilic granulocyte lineage. It is mainly produced by monocytes and macrophages upon activation by endotoxins. Various carcinoma cell lines and myeloblastic leukemia cells can express CSF3 constitutively. In humans, two distinct cDNA clones for CSF3 have been isolated. Both proteins have a 30 amino acid signal peptide and have nearly identical amino acid sequences. Human CSF3 is 73% identical at the amino acid level to murine CSF3 and the two proteins show species cross-reactivity.

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Colony Stimulating Factor 3 (CSF3), formerly called granulocyte colony stimulating factor (G­CSF), is a pleiotropic cytokine. It is mainly produced by monocytes and macrophages upon activation by endotoxin, TNF­α and IFN­γ. Many cell types secreted this protein after LPS, IL1 or TNF­α activation, including fibroblasts, endothelial cells, astrocytes and bone marrow stromal cells. Various carcinoma cell lines and myeloblastic leukemia cells can express CSF3 constitutively. CSF3 is cytokine that acts in hematopoiesis by controlling the production, differentiation and function of 2 related white cell populations of the blood, the granulocytes and the monocytes­macrophages. In addition, it may function in some adhesion or recognition events at the cell surface. The murine CSF3 cDNA encodes a 208 amino acid residue precursor protein containing a 30 amino acid residue signal peptide that is proteolytically cleaved to generate the 178 amino acid residue mature protein. Murine CSF3 is 73% identical at the amino acid level to human CSF3 and the two proteins show species cross­reactivity.

Colony Stimulating Factor 3 (CSF3), formerly called granulocyte colony stimulating factor (G­CSF), is a pleiotropic cytokine. It is mainly produced by monocytes and macrophages upon activation by endotoxin, TNF­α and IFN­γ. Many cell types secreted this protein after LPS, IL1 or TNF­α activation, including fibroblasts, endothelial cells, astrocytes and bone marrow stromal cells. Various carcinoma cell lines and myeloblastic leukemia cells can express CSF3 constitutively. CSF3 is cytokine that acts in hematopoiesis by controlling the production, differentiation and function of two related white cell populations of the blood, the granulocytes and the monocytes­macrophages. In addition, it may function in some adhesion or recognition events at the cell surface.

Colony Stimulating Factor 3 (CSF3), previously known as granulocyte colony stimulating factor (G-CSF) is a pleiotropic cytokine and mainly produced by monocytes and macrophages upon activation by endotoxin, TNF-α and IFN-γ. Many cell types secreted this protein after LPS, IL-1 or TNFα activation, including fibroblasts, endothelial cells, astrocytes and bone marrow stromal cells. Various carcinoma cell lines and myeloblastic leukemia cells can express CSF3 constitutively. CSF3 is cytokine that acts in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytesmacrophages. In addition it may function in some adhesion or recognition events at the cell surface.

KIT Ligand (KITLG), also called Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane SCF is required for normal hematopoietic function. SCF plays an important role in hematopoiesis, spermatogenesis and melanogenesis and it promotes mast cell adhesion, migration, proliferation, and survival. Soluble canine SCF shares 76-93% amino acid sequence identity with many other species, including human, mouse, rat and equine. Cells known to express SCF include endothelial cells, fibroblasts and keratinocytes.

C-kit ligand, the recently identified ligand for the kit tyrosine kinase receptor, is mapped to the mouse S1 locus. This pleiotropic cytokine, alternately known as stem cell factor (SCF), mast cell growth factor (MGF) and steel-factor (SLF), plays essential roles in gametogenesis, melanogenesis and early stages of hematopoiesis. In vitro and in vivo KITLG can stimulate the proliferation of mature, as well as the proliferation and maturation of immature mast cells. KITLG acts in a synergistic manner on purified primitive human and mouse hematopoietic precursors, with various growth factors (such as IL1, IL3, IL6, IL7 and Epo,) to induce myeloid, erythroid and lymphoid lineage colony formation. The finding that KITLG is also expressed in the nervous system suggests a possible role for KITLG in the development of the nervous system.

C-kit ligand, the recently identified ligand for the kit tyrosine kinase receptor, is mapped to the mouse S1 locus. This pleiotropic cytokine, alternately known as stem cell factor (SCF), mast cell growth factor (MGF) and steel-factor (SLF), plays essential roles in gametogenesis, melanogenesis and early stages of hematopoiesis. In vitro and in vivo, KITLG can stimulate the proliferation of mature, as well as the proliferation and maturation of immature, mast cells. KITLG acts in a synergistic manner on purified primitive human and mouse hematopoietic precursors, with various growth factors (such as IL1, IL3, IL6, IL7, and Epo), to induce myeloid, erythroid and lymphoid lineage colony formation. The finding that KITLG is also expressed in the nervous system suggests a possible role for KITLG in the development of the nervous system.

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KIT Ligand (KITLG), also called Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane SCF is required for normal hematopoietic function. SCF plays an important role in hematopoiesis, spermatogenesis and melanogenesis and it promotes mast cell adhesion, migration, proliferation, and survival. Rat KITLG shares 75­-90% amino acid sequence identity with canine, feline, mouse, and human KITLG. Furthermore, rat KITLG is active on mouse and human cells, but human KITLG is only weakly active on mouse cells.

Serpin Peptidase Inhibitory, clade F (SERPINF1), previously called Pigment epithelium-derived factor (PEDF), is encoded by the SERPINF1 gene in humans and found in vertebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. SERPINF1 is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 amino acid, ~50 kDa precursor that contains a 19 amino acid signal sequence and a 399 amino acid mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity, SERPINF1 has induces extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. SERPINF1 is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer.

Thrombopoietin (THPO), the ligand for the receptor encoded by the c-Mpl proto-oncogene, is a key regulator of megakaryocytopoiesis and thrombopoiesis in vitro and in vivo. The cDNAs for THPO have recently been cloned from canine, murine and human sources. The proteins from these three species are highly conserved, exhibiting from 69-75% sequence identity at the amino acid level. Two distinct domains, separated by a pair of arginine residues that may be a proteolytic cleavage site, have been identified in THPO: the amino terminal region exhibiting sequence homology to erythropoietin and the carboxy terminal region containing multiple potential N-linked glycosylation sites. Recombinant THPO has been shown to stimulate the maturation, as well as the proliferation, of megakaryocytes and may have important therapeutic applications for the treatment of various clinical conditions associated with thrombocytopenia.

Thymic stromal lymphopoietin (TSLP) is a hemopoietic protein belonging to the cytokine family and is known to play an important role in the maturation of T cell populations through activation of antigen presenting cells. It is mainly expressed in tissues, including heart, liver and prostate. TSLP signals through a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor and the IL7R alpha chain. Like IL7, TSLP induces phosphorylation of STAT3 and STAT5, but uses kinases other than the JAKs for activation. After binding STAT5, phosphorylation is induced which results in the expression of downstream transcription factors. TSLP enhances the maturation of CD11c+ dendritic cells and induces allergic inflammation by directly activating mast cells. TSLP’s expression is linked to many disease states including asthma, inflammatory arthritis, atopic dermatitis, and eczema and other allergic states but the factors which induce the activation of TSLP release are not clearly defined. Human TSLP shares approximately 43 % amino acid sequence identity with mouse TSLP.