CD115, Recombinant, Human, Fc Chimera (BSA Free) (c-fms, Fms, CSF-1R, M-CSFR)

CD115 is also known as c-fms, marcophage colony stimulating factor receptor, or CSF-1R. It exists in immature (gp130 c-fms) and mature (gp150 c-fms) forms. CSF-1R exhibits an intrinsic tyrosine-specific protein kinase activity. It is expressed on the cells of the mononuclear phagocyte lineage. CSF-1R is an integral transmembrane glycoprotein consisting of a 512 amino acid extracellular domain that includes the CSF-1 binding site, a single 25 amino acid membrane-spanning segment, and a 435 amino acid cytoplasmic portion that includes the tyrosine kinase domain.\n\nA DNA sequence encoding the extracellular domain of human M-CSF R (c-fms) (aa residue 1-512) (Coussens, L. et al., 1986, Nature 320:277-280) was fused to the carboxy-terminal 6X histidine tagged Fc region of human IgG1 via a ploypeptide linker. The chimeric protein was expressed in a mouse myeloma cell line, NSO. Recombinant human M-CSF R/Fc chimera is a disulfide-linked homodimer. Each monomeric subunit, generated after the removal of a 19 residue signal peptide, contains 737 amino acid residues with a calculated molecular mass of 81kD. As a result of glycosylation, the monomeric subunits migrate as an approximately 150kD protein in SDS-PAGE under reducing conditions.\n\nHuman Macrophage Colony Stimulating Factor R/Fc Chimera M-CSF receptor, the product of the c-fms proto-oncogene, is a member of the type III subfamily of receptor tyrosine kinases that\nalso includes Flt-3, the receptor for SCF, and the a and b receptors for PDGF. These receptors are characterized by the presence of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. M-CSF binding induces receptor homodimerization, resulting in transphosphorylation of specific cytoplasmic tyrosine residues and signal transduction. The c-fms proto-oncogene has been mapped to chromosome 5 at band 5q33.3, in close proximity to the gene for the PDGF b receptor. M-CSF receptor is expressed primarily on cells of the monocyte/macrophage lineage and in various tissues of\nthe developing placenta Human M-CSF receptor cDNA encodes a 972 amino acid residue type I membrane protein with a 23 aa residue putative signal peptide, a 489 aa residue extracellular region containing the ligand-binding domain, a 25 aa residue transmembrane domain and a\n435 aa residue cytoplasmic domain. Activators of protein kinase C has been shown to induce the proteolytic cleavage of M-CSF receptor from the cell surface, resulting in the release of the functional ligand-binding extracellular domain. Recombinant soluble M-CSF R/Fc chimera binds M-CSF with high affinity and is a potent M-CSF antagonist (Sherr, C.J. 1990, Blood 75:1-12;\nHamilton, J.A., 1997, J. Leukoc. Biol. 62:145-155).\n\nSource

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

C2447-52E1

Size

100ug

Reactivities

Fel

Form

Supplied as a lyophilized powder from a 0.2um sterile-filtered solution in PBS. It is recommended that sterile PBS containing at least 0.1% HSA or BSA be added to the vial to prepare a stock solution of no less than 50mg/ml. Also available with BSA. See C2447-52E.

Purity

(same/more than) 97%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Sherr, C.J., Blood 75: 1-12 (1990). 2. Hamilton, J.A., J. Leukoc. Biol. 62: 145-155 (1997).