Ambient

m-Cresol, High Purity

m-Cresol, High Purity

m-Cresol, High Purity

m-Cresol, High Purity

m-Cresol, High Purity

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.

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.

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.

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.

Molecular Formula : C27 H33 O4 P

Molecular Formula : C27 H33 O4 P

Molecular Formula : C27 H33 O4 P

Molecular Formula : C10 H14

Molecular Formula : C10 H14

Molecular Formula : C18H18FNO2S

Molecular Formula : C18H18FNO2S

Molecular Formula : C11H17NO2

Molecular Formula : C11H17NO2

Molecular Formula : C11H17NO2

m-Hydroxybenzoic Acid

m-Hydroxybenzoic Acid

m-Hydroxybenzoic Acid

Molecular Formula : C17 H21 N O5

Molecular Formula : C17 H21 N O5

Molecular Formula : C17H18D3NO5

Molecular Formula : C17H18D3NO5

Molecular Formula : C9H9NO4

Molecular Formula : C9H9NO4

Molecular Formula : C713C2H915NO4

Molecular Formula : C713C2H915NO4

Molecular Formula : C13 H18 O2

Molecular Formula : C13 H18 O2

Molecular Formula : C9H13NO

Molecular Formula : C9H13NO

Molecular Formula : C9H13NO

GenScript M-MuLV Reverse Transcriptase (M-MLV) is derived from a cloned region of the pol gene of MMLV and isolated from an E. coli strain overexpressing this construct. To increase cDNA yields and get a higher percentage of longer transcripts, the M-MLV Reverse Transcriptase has been modified with reduced RNase H activity, and expressed free of exogenous RNases and other nucleases. The enzyme can synthesize a complementary cDNA strand initiating from a primer using RNA as template (cDNA synthesis), making it ideal for a wide range of applications.

GenScript M-MuLV Reverse Transcriptase (M-MLV) is derived from a cloned region of the pol gene of MMLV and isolated from an E. coli strain overexpressing this construct. To increase cDNA yields and get a higher percentage of longer transcripts, the M-MLV Reverse Transcriptase has been modified with reduced RNase H activity, and expressed free of exogenous RNases and other nucleases. The enzyme can synthesize a complementary cDNA strand initiating from a primer using RNA as template (cDNA synthesis), making it ideal for a wide range of applications.