CD115 (CSF1R) ELISA Kit for Mouse

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: EC 2.7.10.1; Oncoprotein; Membrane protein, integral; Protein kinase, TK; Protein kinase, tyrosine (receptor); Kinase, protein; 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; cytokine binding; protein-tyrosine kinase activity; transferase activity, transferring phosphorus-containing groups; kinase activity; ATP binding

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