CD115 Antibody – Rat Monoclonal

CSFR: an oncogenic tyrosine kinase receptor for CSF-1 (M-CSF). Drives growth and development of monocytes. Binding of CSF-1 induces receptor dimerization, activation and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins. There are at least five major tyrosine autophosphorylation sites. Two point mutations seen in 10-20% of patients with acute myeloid leukemia, chronic myelomonocytic leukemia or myelodysplasia. One mutation appears to be both somatic and germline, and disrupts Cbl binding and receptor turnover. v-fms lacks the Cbl binding site and causes feline leukemia. Mutations may also develop after chemotherapy for lymphoma. A distinct point mutation was found in some cases of hepatocellular carcinoma and related to increased expression, and another mutation was found in 2 of 40 patients with idiopathic myelofibrosis. Expression is elevated in breast tumors and cell lines, and expression in xenografts and transgenic mice has been correlated with xenograft growth and breast cancer development. Inhibitors: Ki-20227 and other Kit/PDGFR inhibitors.

Protein type: Protein kinase, TK; Kinase, protein; Oncoprotein; Protein kinase, tyrosine (receptor); EC 2.7.10.1; Membrane protein, integral; TK group; PDGFR family

Cellular Component: cell surface; membrane; integral to membrane; plasma membrane; intracellular; receptor complex

Molecular Function: macrophage colony stimulating factor receptor activity; protein homodimerization activity; nucleotide binding; transmembrane receptor protein tyrosine kinase activity; protein phosphatase binding; protein kinase activity; transferase activity; protein binding; protein-tyrosine kinase activity; cytokine binding; transferase activity, transferring phosphorus-containing groups; kinase activity; ATP binding

Biological Process: regulation of bone resorption; peptidyl-tyrosine phosphorylation; phosphoinositide-mediated signaling; immune system process; positive regulation of osteoclast differentiation; protein amino acid autophosphorylation; cytokine and chemokine mediated signaling pathway; osteoclast differentiation; protein amino acid phosphorylation; positive regulation of tyrosine phosphorylation of Stat3 protein; cell proliferation; regulation of cell shape; positive regulation of cell proliferation; ruffle organization and biogenesis; innate immune response; hemopoiesis; phosphatidylinositol metabolic process; positive regulation of protein amino acid phosphorylation; intercellular junction maintenance; inflammatory response; phosphorylation; transmembrane receptor protein tyrosine kinase signaling pathway; positive regulation of cell migration