Csf1r (P909) Blocking Peptide | Csf1r blocking peptide

Mouse Csf1r Blocking Peptide (P909)

• Gene Names: Csf1r; Fms; Fim2; CD115; Csfmr; Fim-2; CSF-1R; M-CSFR; M-CSF-R; AI323359
• Synonyms: Csf1r (P909); Mouse Csf1r Blocking Peptide (P909); Macrophage colony-stimulating factor 1 receptor; CSF-1 receptor; CSF-1-R; CSF-1R; M-CSF-R; Proto-oncogene c-Fms; CD115; Csf1r; Csfmr; Fms; Csf1r blocking peptide

• Specificity: The synthetic peptide sequence is selected from aa 910-920 of HUMAN Csf1r
• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 977

• Cellular Location: Cell membrane; Single-pass type I membrane protein Note: The autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation
• Tissue Location: Widely expressed.
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for Csf1r blocking peptide

Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5- trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP- 1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor.

NCBI and Uniprot Product Information

• NCBI GI #: 20532397
• NCBI GeneID: 12978
• UniProt Accession #: P09581; Q3U3P1; Q9DBH9
• Molecular Weight: 109,179 Da
• NCBI Official Full Name: Macrophage colony-stimulating factor 1 receptor
• NCBI Official Synonym Full Names: colony stimulating factor 1 receptor
• NCBI Official Symbol: Csf1r
• NCBI Official Synonym Symbols: Fms; Fim2; CD115; Csfmr; Fim-2; CSF-1R; M-CSFR; M-CSF-R; AI323359
• NCBI Protein Information: macrophage colony-stimulating factor 1 receptor
• UniProt Protein Name: Macrophage colony-stimulating factor 1 receptor
• Protein Family: Macrophage colony-stimulating factor 1 receptor
• UniProt Gene Name: Csf1r
• UniProt Synonym Gene Names: Csfmr; Fms; CSF-1-R; CSF-1R; M-CSF-R
• UniProt Entry Name: CSF1R_MOUSE

Uniprot Description

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

Cellular Component: cell surface; membrane; plasma membrane

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

Biological Process: axon guidance; cell proliferation; cytokine and chemokine mediated signaling pathway; forebrain neuron differentiation; hemopoiesis; 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; 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; regulation of bone resorption; regulation of cell shape; ruffle organization and biogenesis; transmembrane receptor protein tyrosine kinase signaling pathway