- CITATIONS: 1
|Application ||FC, WB, IHC-P, E|
|Calculated MW||107984 Da|
|Antigen Region||940-971 aa|
|Other Names||Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor, CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS|
|Target/Specificity||This MCSF Receptor (CSF1R) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 940-971 amino acids from the C-terminal region of human MCSF Receptor (CSF1R).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MCSF Receptor (CSF1R) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Expressed in bone marrow and in differentiated blood mononuclear cells|
Provided below are standard protocols that you may find useful for product applications.
CSF1R is the receptor for colony stimulating factor 1, a cytokine which controls the production, differentiation, and function of macrophages. This receptor mediates most if not all of the biological effects of this cytokine. Ligand binding activates the receptor kinase through a process of oligomerization and transphosphorylation. This protein is a tyrosine kinase transmembrane receptor and member of the CSF1/PDGF receptor family of tyrosine-protein kinases. Mutations in the gene encoding CSF1R have been associated with a predisposition to myeloid malignancy.
Follows, G.A., et al., EMBO J. 22(11):2798-2809 (2003).
Riccioni, R., et al., Leukemia 17(1):98-113 (2003).
Zhu, K., et al., Biochem. Biophys. Res. Commun. 297(5):1211-1217 (2002).
Ide, H., et al., Proc. Natl. Acad. Sci. U.S.A. 99(22):14404-14409 (2002).
Flick, M.B., et al., J. Cell. Biochem. 85(1):10-23 (2002).
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