10g

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.

Molecular Formula : C5H7ClO3

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

Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine that was previously called monocyte-specific chemokine 3 (MCP-3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature form, it is classified within the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, within a large cluster containing many other CC chemokines and is most closely related to CCL2. CCL7 can signal through the CCR1, CCR2 and CCR3 receptors.

Mecobalamin, JP

Methyl 4-(Bromomethyl)benzoate

Methyl Alcohol-d4, 99.8 Atom Percent D

Methyl N,N-Dimethylanthranilate

Methyl-beta-cyclodextrin