Detection of Human M-CSF R/CD115 by Western Blot.|
Western blot shows lysates of THP‑1 human acute monocytic leukemia cell line. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human M-CSF R/CD115 Monoclonal Antibody (Catalog # MAB3291) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for M-CSF R/CD115 at approximately 130 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
M-CSF R/CD115 Inhibition of M-CSF-dependent Cell Proliferation and Neutralization by Human|
M-CSF R/CD115 Antibody. Recombinant Human
M-CSF R/CD115 Fc Chimera (Catalog # 329-MR) inhibits Recombinant Human M-CSF (Catalog # 216-MC) induced proliferation in the M‑NFS‑60 mouse myelogenous leukemia lymphoblast cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Human M-CSF R/CD115 (1 ng/mL) activity elicited by Recombinant Human
M-CSF R/CD115 Fc Chimera (30 ng/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human M-CSF R/CD115 Monoclonal Antibody (Catalog # MAB3291). The ND50 is typically 4-16 ng/mL.
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).
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