10g
Showing 3301–3350 of 4637 results
-
Lead Acetate Trihydrate
Molecular Formula : C4H6O4Pb . 3H2O
-
Lead Powder, -200 mesh
Molecular Formula : Pb
-
Lead Titanium Zirconium Oxide (~30% by weight)
Molecular Formula : O3 Pb Ti(x) Zr(y)
-
Lead(II) Chromate
Molecular Formula : CrO4Pb
-
Lead(II) Nitrate
Molecular Formula : 2 N O3 . Pb
-
Lead(II) Oxide
Molecular Formula : PbO
-
Lead(IV) Acetate, Stabilized
Molecular Formula : C8 H12 O8 Pb
-
Lentinan (Technical Grade)
Molecular Formula : (C42H70O35)nH2O
-
Leucomycins (>85%)
Molecular Formula : No Data Available
-
Levamisole Hydrochloride
Levamisole Hydrochloride
-
Lidocaine
Molecular Formula : C14 H22 N2 O
-
Lidocaine Hydrochloride Monohydrate
Molecular Formula : C14 H22 N2 O . Cl H . H2 O
-
LIF, Human
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.
-
LIF, Mouse
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
Light Green SF Yellowish
-
Linalool
Molecular Formula : C10 H18 O
-
Lindane
Molecular Formula : C6 H6 Cl6
-
Linoleic Acid
Molecular Formula : C18 H32 O2
-
Linoleic Acid
Linoleic Acid
-
Lithium Dodecyl Sulfate
Lithium Dodecyl Sulfate
-
Lithium Fluoride
Molecular Formula : LiF
-
Lithium Perchlorate
Molecular Formula : ClO4 .Li
-
Lithium sulfate, anhydrous
Molecular Formula : Li2SO4
-
Lithium Trifluoromethylsulfonate
Molecular Formula : CF3LiO3S
-
LIX/CXCL5 (74aa), Mouse
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.
-
Longifolene (>75%)
Molecular Formula : C15 H24
-
Lufenuron
Molecular Formula : C17 H8 Cl2 F8 N2 O3
-
Lumazine
Molecular Formula : C6 H4 N4 O2
-
Luminol
Molecular Formula : C8 H7 N3 O2
-
Lyral, mixture of isomers
Molecular Formula : C13 H22 O2
-
m-Aminophenyl Tosylate
Molecular Formula : C13H13NO3S
-
m-Chloro Hippuric Acid
Molecular Formula : C9H8ClNO3
-
m-Cresol Purple
m-Cresol Purple
-
m-Cresol Purple
Molecular Formula : C21H18O5S
-
M-CSF, Human
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.
-
M-CSF, Human(CHO-expressed)
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.
-
M-CSF, Mouse
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.
-
M-CSF, Mouse
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.
-
M-CSF, Rat
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.
-
m-Nitrobenzoic Acid
Molecular Formula : C7 H5 N O4
-
m-Toluoyl Chloride
Molecular Formula : C8H7ClO
-
m-Toluquinoline
Molecular Formula : C10 H9 N
-
Magnesium Ascorbyl Phosphate
Magnesium Ascorbyl Phosphate
-
Magnesium Carbonate
Molecular Formula : C O3 . Mg
-
Magnesium Citrate xHydrate
Molecular Formula : C6H8O7.3/2Mg.XH2O
-
Magnesium Oxide (Technical Grade)
Molecular Formula : Mg O
-
Magnesium Sulfate
Molecular Formula : MgSO4
-
Magnesium Valproate
Molecular Formula : C16 H30 Mg O4
-
Malachite Green Oxalate
Molecular Formula : 2 C23 H25 N2 . C2 H2 O4 . 2 C2 H O4
-
Malachite Green Oxalate
Malachite Green Oxalate