Recombinant Human M-CSF R/CD115 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit the M-CSF-induced proliferation of M‑NFS‑60 mouse myelogenous leukemia lymphoblast cells. Halenbeck, R. et al. (1989) Biotechnology 7:710. The ED50 for this effect is 0.004-0.012 µg/mL in the presence of 1 ng/mL of Recombinant Human M-CSF (Catalog # 216-MC).
Source
Mouse myeloma cell line, NS0-derived human M-CSF R/CD115 protein
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
81 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
109-128 kDa, reducing conditions
Publications
Read Publications using 329-MR/CF in the following applications:
M-CSF receptor, the product of the c-fms proto-oncogene, is a member of the type III subfamily of receptor tyrosine kinases that also includes receptors for SCF and PDGF. These receptors each contain five immunoglobulin-like domains in their extracellular domain (ECD) and a split kinase domain in their intracellular region (1-4). M-CSF receptor is expressed primarily on cells of the monocyte/macrophage lineage, dendritic cells, stem cells and in the developing placenta (1). Human M-CSF receptor cDNA encodes a 972 amino acid (aa) type I membrane protein with a 19 aa signal peptide, a 493 aa extracellular region containing the ligand-binding domain, a 25 aa transmembrane domain and a 435 aa cytoplasmic domain. The human M-CSF R ECD shares 60%, 64%, 72%, 75%, 75% and 76% aa identity with mouse, rat, bovine, canine, feline and equine M-CSF R, respectively. Activators of protein kinase C induce TACE/ADAM17 cleavage of the M-CSF receptor, releasing the functional ligand-binding extracellular domain (5). M-CSF binding induces receptor homodimerization, resulting in transphosphorylation of specific cytoplasmic tyrosine residues and signal transduction (6). The intracellular domain of activated M-CSF R binds more than 150 proteins that affect cell proliferation, survival, differentiation and cytoskeletal reorganization. Among these, PI3Kinase, P42/44 ERK and c-Cbl are key transducers of M-CSF R signals (3, 4). M-CSF R engagement is continuously required for macrophage survival and regulates lineage decisions and maturation of monocytes, macrophages, osteoclasts and DC (3, 4). M-CSF R and integrin alpha v beta 3 share signaling pathways during osteoclastogenesis and deletion of either causes osteopetrosis (7, 8). In the brain, microglia expressing increased M-CSF R are concentrated with Alzheimers a beta peptide, but their role in pathogenesis is unclear (9, 10).
deParseval, N. et al. (1993) Nucleic Acids Res. 21:750.
Rothwell, V.M. and L.R. Rohrschneider (1987) Oncogene Res. 1:311.
Chitu, V. and E.R. Stanley (2006) Curr. Opin. Immunol. 18:39.
Ross, F.P. and S.L. Teitelbaum (2005) Immunol. Rev. 208:88.
Rovida, E. et al. (2001) J. Immunol. 166:1583.
Yeung, Y. et al. (1998) J. Biol. Chem. 273:17128.
Dai, X. et al. (2002) Blood 99:111.
Faccio, R. et al. (2003) J. Clin. Invest. 111:749.
Li, M. et al. (2004) J. Neurochem. 91:623.
Mitrasinovic, O.M. et al. (2005) J. Neurosci. 25:4442.
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