Human Macrophage Colony Stimulating Factor Recombinant

Catalog #
90215-A
$130 *
Size: 2 µg
Qty
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Description

Recombinant Human M-CSF is a disulfide-linked homodimeric protein consisting of two 149 amino acid residues, and migrates as an approximately 42 kDa protein under non-reducing and as 20-21 kDa under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human M-CSF extracellular domain was expressed in E. coli.

Synonyms
M-CSF, Macrophage Colony Stimulating Factor, MCSF, CSF-1, CSF1, Colony Stimulating Factor 1
Product Info
Storage and Usage
Citations
Species
Human
Host Species/Expression System
E. coli
Purity
≥95% by SDS-PAGE and HPLC
Format
lyophilized protein
Formulation

Recombinant CSF1 lyophilized from a 0.2 µm filtered PBS solution pH 7.4 

MW
21 kDa
Endotoxin Level
Endotoxin level was found to be < 0.1 ng/μg (1EU/μg), using the LAL gel clot method.
Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of  of M-NFS-60 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.
UniProt #
P09603
Background
M-CSF is produced by monocytes, granulocytes, endothelial cells, and fibroblasts. After cell activation, B-cells and T- cells and also a number of tumor cell lines are capable also of synthesizing this factor. M-CSF has been found to be synthesized by uterine epithelial cells in vivo. The M-CSF receptor (CD115) is identical with the proto-oncogene fms. The receptor is a transmembrane protein with an extracellular ligand-binding domain of 512 amino acids, an intramembrane domain of 25 amino acids, and a cytoplasmic domain of 435 amino acids encoding a tyrosine kinase. Human M-CSF is active in mouse and rat cells. The murine factor is active in rat cells but inactive in human cells. M-CSF is a specific factor in that the proliferation inducing activity is more or less restricted to the macrophage lineage. M-CSF is a potent stimulator of functional activities of monocytes.
References
1. J. Exp. Med., May 2009, 206: 1089 - 1102.
2. J. Leukoc. Biol., Feb 2009, 85: 262 - 267.
3. Blood (ASH Annual Meeting Abstracts), Nov 2008, 112: 2887.