10g

Molecular Formula : C16 H33 N O2

Molecular Formula : C4H6O4Pb . 3H2O

Molecular Formula : O3 Pb Ti(x) Zr(y)

Molecular Formula : CrO4Pb

Molecular Formula : 2 N O3 . Pb

Molecular Formula : PbO

Molecular Formula : C8 H12 O8 Pb

Molecular Formula : (C42H70O35)nH2O

Levamisole Hydrochloride

Molecular Formula : C14 H22 N2 O

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

Molecular Formula : C10 H18 O

Molecular Formula : C6 H6 Cl6

Molecular Formula : C18 H32 O2

Linoleic Acid

Lithium Dodecyl Sulfate

Molecular Formula : LiF

Molecular Formula : ClO4 .Li

Molecular Formula : Li2SO4

Molecular Formula : CF3LiO3S

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.

Molecular Formula : C15 H24

Molecular Formula : C17 H8 Cl2 F8 N2 O3

Molecular Formula : C6 H4 N4 O2

Molecular Formula : C8 H7 N3 O2

Molecular Formula : C13 H22 O2

Molecular Formula : C13H13NO3S

Molecular Formula : C9H8ClNO3

Molecular Formula : C21H18O5S

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

Molecular Formula : C O3 . Mg

Molecular Formula : Mg O

Molecular Formula : MgSO4

Molecular Formula : C16 H30 Mg O4

Molecular Formula : 2 C23 H25 N2 . C2 H2 O4 . 2 C2 H O4

Malachite Green Oxalate

Molecular Formula : C5H6O4

Molecular Formula : C4 H2 O3

Molecular Formula : C4H3NO2

Molecular Formula : C3H2Na2O4 . H2O

Molecular Formula : C3 H2 N2