10g

Interleukin-3 (IL-3) is a pleiotropic cytokine belonging to the interleukin family. IL-3 shares similarities with Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF) and IL-5: they all have a four-helix bundle structure, are located on the same chromosomes in both human and mouse, are produced by activated T cells, and share receptors. The IL-3/IL-5/GM-CSF receptor family members are all heterodimeric, composed of a receptor-specific α chain and a common β chain. IL-3 is also called multi-colony stimulating factor since it stimulates the development and colony formation of multiple lineages of hematopoietic cells by activating intracellular pathways such as Ras-Raf-ERK and JAK/STAT. IL-3 inhibits apoptosis and promotes cell survival by targeting the anti-apoptotic bcl-2 gene family.

Interleukin-3 (IL-3) is a pleiotropic cytokine belonging to the interleukin family. IL-3 shares similarities with Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF) and IL-5: they all have a four-helix bundle structure, are located on the same chromosomes in both human and mouse, are produced by activated T cells, and share receptors. The IL-3/IL-5/GM-CSF receptor family members are all heterodimeric, composed of a receptor-specific α chain and a common β chain. IL-3 is also called multi-colony stimulating factor since it stimulates the development and colony formation of multiple lineages of hematopoietic cells by activating intracellular pathways such as Ras-Raf-ERK and JAK/STAT. IL-3 inhibits apoptosis and promotes cell survival by targeting the anti-apoptotic bcl-2 gene family.

Interleukin-3 (IL-3) is a pleiotropic cytokine belonging to the interleukin family. IL-3 shares similarities with Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF) and IL-5: they all have a four-helix bundle structure, are located on the same chromosomes in both human and mouse, are produced by activated T cells, and share receptors. The IL-3/IL-5/GM-CSF receptor family members are all heterodimeric, composed of a receptor-specific α chain and a common β chain. IL-3 is also called multi-colony stimulating factor since it stimulates the development and colony formation of multiple lineages of hematopoietic cells by activating intracellular pathways such as Ras-Raf-ERK and JAK/STAT. IL-3 inhibits apoptosis and promotes cell survival by targeting the anti-apoptotic bcl-2 gene family.

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-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-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 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 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.

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 Receptor Alpha, also known as IL-6RA, IL-6R1 and CD126, belongs to the type I cytokine receptor family. It is mainly expressed on T cells, fibroblasts and macrophages. IL-6RA couples with gp130 to form the IL-6 receptor; IL-6RA binds specifically to IL-6 and depends on gp130 to transmit signals. IL-6RA dysfunction has been correlated with the pathogenesis of many diseases, such as multiple myeloma, autoimmune diseases and prostate cancer. Soluble IL-6RA, which consists of only the extracellular domain of IL-6RA, acts as an agonist of IL-6 activity.

Interleukin-7 (IL-7), also known as lymphopoietin 1 and pre-B cell factor, is a hematopoietic growth factor belonging to the IL-7/IL-9 family. It is produced by keratinocytes, dendritic cells, hepatocytes, neurons and epithelial cells. IL-7 binds and signals through IL-7 receptor, a heterodimer consisting of IL-7 receptor alpha and common gamma chain receptor. IL-7 plays a role in regulating early B cell and T cell development. It is also important for optimal dendritic cell-T cell interaction.

Interleukin-7 (IL-7), also known as lymphopoietin 1 and pre-B cell factor, is a hematopoietic growth factor belonging to the IL-7/IL-9 family. It is produced by keratinocytes, dendritic cells, hepatocytes, neurons and epithelial cells. IL-7 binds and signals through IL-7 receptor, a heterodimer consisting of IL-7 receptor alpha and common gamma chain receptor. IL-7 plays a role in regulating early B cell and T cell development. It is also important for optimal dendritic cell-T cell interaction.

Interleukin-8 (IL-8), also known as CXCL8, GCP-1 and NAP-1, is one of the first discovered chemokines and belongs to the CXCL family, in which the first two conserved cysteines are separated by one residue. In vivo, IL-8 exists in two forms: a 77 a.a. protein produced by endothelial cells, and the more active 72 a.a. protein produced by monocytes. The receptors for IL-8 are the seven-helical G-protein coupled receptors CXCR1 and CXCR2, exclusively expressed on neutrophils. The functions of IL-8 are to induce rapid changes in cell morphology, activate integrins, and release the granule contents of neutrophils. Thus, IL-8 can enhance the antimicrobial actions of defense cells. It is secreted by monocytes, macrophages and endothelial cells. IL-8 signals through CXCR1 and CXCR2 to chemoattract neutrophils, basophils, and T cells. IL-8 is also a potent promoter of angiogenesis. Other functions of this protein, such as involvement in bronchiolitis pathogenesis, have also been reported.

Interleukin 9, also known as IL9, is a cytokine (cell signalling molecule) belonging to the group of interleukins. The protein encoded by this gene is a cytokine produced by T-cells and specifically by CD4+ helper cells that acts as a regulator of a variety of hematopoietic cells. This cytokine stimulates cell proliferation and prevents apoptosis. It functions through the interleukin-9 receptor (IL9R), which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

Interleukin 9, also known as IL9, is a cytokine (cell signalling molecule) belonging to the group of interleukins. The protein encoded by this gene is a cytokine produced by T-cells and specifically by CD4+ helper cells that acts as a regulator of a variety of hematopoietic cells. This cytokine stimulates cell proliferation and prevents apoptosis. It functions through the interleukin-9 receptor (IL9R), which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

Iodocyclohexane, (stabilized with Copper chip)

IP-10/CXCL10 also known as CXCL10, is originally identified as an IFN-γ-inducible gene in monocytes, fibroblasts and endothelial cells. It has since been shown that IP-10 mRNA is also induced by LPS, IL-1β, TNF-α, IL-12 and viruses. Additional cell types that have been shown to express IP-10 include activated T-lymphocytes, splenocytes, keratinocytes, osteoblasts, astrocytes, and smooth muscle cells. IP-10 is also expressed in psoriatic and lepromatous lesions of skin. The mouse homologue of human IP-10, Crg-2, has been cloned and shown to share approximately 67% amino acid sequence identity with human IP-10.

Isoluminol, [Chemiluminescence reagent]

Jenner Stain

Kanamycin Sulfate

Keratinocyte Growth Factor (KGF) is a highly specific epithelial mitogen produced by fibroblasts and mesenchymal stem cells. KGF belongs to the heparin binding Fibroblast Growth Factor (FGF) family, and is known as FGF-7. However, in contrast to the FGF-1, which binds to all known FGF receptors with high affinity, KGF only binds to a splice variant of an FGF receptor, FGFR2-IIIb. FGFR2-IIIb is produced by most of the epithelial cells, indicating that KGF plays roles as a paracrine mediator. KGF induces the differen-tiation and proliferation of various epithelial cells, including keratinocytes in the epidermis, hair follicles and sebaceous glands, and is responsible for the wound repairs of various tissues, including lung, bladder, and kidney.

Keratinocyte Growth Factor (KGF) is a highly specific epithelial mitogen produced by fibroblasts and mesenchymal stem cells. KGF belongs to the heparin binding Fibroblast Growth Factor (FGF) family, and is known as FGF-7. However, in contrast to FGF-1, which binds to all known FGF receptors with high affinity, KGF only binds to a splice variant of the FGF receptor, FGFR2-IIIb. FGFR2-IIIb is expressedby most epithelial cells, indicating KGF’s roleas a paracrine mediator. KGF induces the differentiation and proliferation of various epithelial cells such as keratinocytes in the epidermis, hair follicles and sebaceous glands., KGF is also responsible for wound repair of various tissuesincluding lung, bladder, and kidney.

L-Glutathione, Oxidized

L-Tyrosine Ethyl Ester

Levamisole Hydrochloride

Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine belonging to the long four-helix bundle cytokine superfamily. LIF shares tertiary structure with several other cytokines, including Interleukin-6 (IL-6), Oncostatin M, ciliary neurotropic factor, and cardiotrophin-1, and their functions in vivo are also redundant to some extent. LIF can bind to the common receptor of IL-6 subfamily, gp130, and then recruit its own receptor LIF Receptor to form a ternary complex. The basal expression of LIF in vivo is low; and its expression is induced by pro-inflammatory factors, including lipopolysaccharide, IL-1, and IL-17, and inhibited by anti-inflammatory agents, including IL-4 and IL-13. The functions of LIF include proliferation of primordial germ cells, regulation in blastocyst implantation and early pregnancy, and maintenance of pluripotent embryonic stem cells.

Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine belonging to the long four-helix bundle cytokine superfamily. LIF shares tertiary structure with several other cytokines, including Interleukin-6 (IL-6), Oncostatin M, ciliary neurotropic factor, and cardiotrophin-1, and their functions in vivo are also redundant to some extent. LIF can bind to the common receptor of IL-6 subfamily, gp130, and then recruit its own receptor LIF Receptor to form a ternary complex. The basal expression of LIF in vivo is low; and its expression is induced by pro-inflammatory factors, including lipopolysaccharide, IL-1, and IL-17, and inhibited by anti-inflammatory agents, including IL-4 and IL-13. The functions of LIF include proliferation of primordial germ cells, regulation in blastocyst implantation and early pregnancy, and maintenance of pluripotent embryonic stem cells.

Light Green SF Yellowish

Linoleic Acid

Lithium Dodecyl Sulfate

Mouse LIX (C-X-C motif chemokine 5) is a small cytokine belonging to the CXC chemokine family that is cleaved into the following 2 chains [GCP-2(1-78) and GCP-2(9-78)]. Mouse LIX plays a role in reducing sensitivity to sunburn pain in some subjects, and is a potential target which could be used to understand more about pain in other inflammatory conditions. It is most closely related to two highly homologous human neutrophil chemoattractants GCP-2 and ENA-78. The first 78 amino acid residues within the predicted mature mouse LIX shares approximately 61% and 55% amino acid identity with human GCP-2 and ENA-78. This chemokine stimulates the chemotaxis of neutrophils possessing angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2.

m-Cresol Purple

Macrophage-Colony Stimulating Factor (M-CSF), also known as Colony Stimulating Factor-1 (CSF-1), is a hematopoietic growth factor. It can stimulate the survival, proliferation and differentiation of mononuclear phagocytes, in addition to the spreading and motility of macrophages. In mammals, it exits three isoforms, which invariably share an N-terminal 32-aa signal peptide, a 149-residue growth factor domain, a 21-residue transmembrane region and a 37-aa cytoplasmictail. M-CSF is mainly produced by monocytes, macrophages, fibroblasts, and endothelial cells. M-CSF interaction with its receptor, c-fms, has been implicated in the growth, invasion, and metastasis of of several diseases, including breast and endometrial cancers. The biological activity of human M-CSF is maintained within the 149-aa growth factor domain, and it is only active in the disulfide-linked dimeric form, which is bonded at Cys63.

Macrophage-Colony Stimulating Factor (M-CSF), also known as Colony Stimulating Factor-1 (CSF-1), is a hematopoietic growth factor. It can stimulate the survival, proliferation and differentiation of mononuclear phagocytes, in addition to the spreading and motility of macrophages. In mammals, it exits three isoforms, which invariably share an N-terminal 32-aa signal peptide, a 149-residue growth factor domain, a 21-residue transmembrane region and a 37-aa cytoplasmictail. M-CSF is mainly produced by monocytes, macrophages, fibroblasts, and endothelial cells. M-CSF interaction with its receptor, c-fms, has been implicated in the growth, invasion, and metastasis of of several diseases, including breast and endometrial cancers. The biological activity of human M-CSF is maintained within the 149-aa growth factor domain, and it is only active in the disulfide-linked dimeric form, which is bonded at Cys63.

Macrophage-Colony Stimulating Factor (M-CSF), also known as Colony Stimulating Factor-1 (CSF-1), is a hematopoietic growth factor. It can stimulate the survival, proliferation and differentiation of mononuclear phagocytes, in addition to the spreading and motility of macrophages. In mammals, it exits three isoforms, which invariably share an N-terminal 32-aa signal peptide, a 149-residue growth factor domain, a 21-residue transmembrane region and a 37-aa cytoplasmictail. M-CSF is mainly produced by monocytes, macrophages, fibroblasts, and endothelial cells. M-CSF interaction with its receptor, c-fms, has been implicated in the growth, invasion, and metastasis of of several diseases, including breast and endometrial cancers. The biological activity of human M-CSF is maintained within the 149-aa growth factor domain, and it is only active in the disulfide-linked dimeric form, which is bonded at Cys63.

Macrophage-Colony Stimulating Factor (M-CSF), also known as Colony Stimulating Factor-1 (CSF-1), is a hematopoietic growth factor. It can stimulate the survival, proliferation and differentiation of mononuclear phagocytes, in addition to the spreading and motility of macrophages. In mammals, it exits three isoforms, which invariably share an N-terminal 32-aa signal peptide, a 149-residue growth factor domain, a 21-residue transmembrane region and a 37-aa cytoplasmictail. M-CSF is mainly produced by monocytes, macrophages, fibroblasts, and endothelial cells. M-CSF interaction with its receptor, c-fms, has been implicated in the growth, invasion, and metastasis of of several diseases, including breast and endometrial cancers. The biological activity of human M-CSF is maintained within the 149-aa growth factor domain, and it is only active in the disulfide-linked dimeric form, which is bonded at Cys63.

Macrophage-Colony Stimulating Factor (M-CSF), also known as Colony Stimulating Factor-1 (CSF-1), is a hematopoietic growth factor. It can stimulate the survival, proliferation and differentiation of mononuclear phagocytes, in addition to the spreading and motility of macrophages. In mammals, it exits three isoforms, which invariably share an N-terminal 32-aa signal peptide, a 149-residue growth factor domain, a 21-residue transmembrane region and a 37-aa cytoplasmictail. M-CSF is mainly produced by monocytes, macrophages, fibroblasts, and endothelial cells. M-CSF interaction with its receptor, c-fms, has been implicated in the growth, invasion, and metastasis of of several diseases, including breast and endometrial cancers. The biological activity of human M-CSF is maintained within the 149-aa growth factor domain, and it is only active in the disulfide-linked dimeric form, which is bonded at Cys63.

Magnesium Ascorbyl Phosphate

Malachite Green Oxalate