CSF1R Antibody – Rabbit Polyclonal

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

Cellular Component: cell surface; membrane; integral to membrane; plasma membrane

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

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

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

Cellular Component: cell surface; integral to membrane; membrane; plasma membrane

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

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