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CSF1R/MCSF Receptor/CD115 Protein, Antibody, ELISA Kit, cDNA Clone

Mouse CSF1R/MCSF Receptor/CD115 Protein

Expression host: Human Cells
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50059-M03H-50
50059-M03H-100
50 µg / $178
100 µg / $298
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Description: Active
Expression host: Human Cells
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50059-M08H-50
50059-M08H-100
50 µg / $198
100 µg / $348
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Rat CSF1R/MCSF Receptor/CD115 Protein

Expression host: Human Cells
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80447-R08H-50
80447-R08H-100
50 µg / $178
100 µg / $298
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Expression host: Human Cells
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80447-R02H-50
80447-R02H-100
50 µg / $198
100 µg / $298
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Human CSF1R/MCSF Receptor/CD115 Protein

Description: Active
Expression host: Human Cells
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10161-H03H-100
10161-H03H-200
100 µg / $198
200 µg / $298
Add to Cart
Expression host: Human Cells
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10161-HCCH-100
10161-HCCH-200
100 µg / $178
200 µg / $298
Add to Cart
Description: Active
Expression host: Human Cells
  • Slide 1
  • Slide 1
10161-H08H-50
10161-H08H-100
50 µg / $108
100 µg / $178
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Expression host: Baculovirus-Insect Cells
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10161-H20B1-20
10161-H20B1-100
20 µg / $138
100 µg / $348
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Expression host: Baculovirus-Insect Cells
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10161-H20B2-20
10161-H20B2-100
20 µg / $138
100 µg / $348
Add to Cart

CSF1R/MCSF Receptor/CD115 Related Areas

CSF1R/MCSF Receptor/CD115 Related Pathways

CSF1R/MCSF Receptor/CD115 Related Product

CSF1R/MCSF Receptor/CD115 Summary & Protein Information

CSF1R/MCSF Receptor/CD115 Related Information

CSF1R/MCSF Receptor/CD115 Background

Gene Summary: The protein encoded by CSF1R gene 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. The encoded protein is a tyrosine kinase transmembrane receptor and member of the CSF1/PDGF receptor family of tyrosine-protein kinases. Mutations in CSF1R gene have been associated with a predisposition to myeloid malignancy. The first intron of CSF1R gene contains a transcriptionally inactive ribosomal protein L7 processed pseudogene oriented in the opposite direction. [provided by RefSeq, Jul 2008]
General information above from NCBI
Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation: Present in an inactive conformation in the absence of bound ligand. CSF1 or IL34 binding leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib/STI-571 (Gleevec), dasatinib, sunitinib/SU11248, lestaurtinib/CEP-701, midostaurin/PKC-412, Ki20227, linifanib/ABT-869, Axitinib/AG013736, sorafenib/BAY 43- 9006 and GW2580.
Subunit structure: Interacts with INPPL1/SHIP2 and THOC5 (By similarity). Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts (tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts (tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with CBL, GRB2 and SLA2.
Domain: The juxtamembrane domain functions as autoinhibitory region. Phosphorylation of tyrosine residues in this region leads to a conformation change and activation of the kinase.
The activation loop plays an important role in the regulation of kinase activity. Phosphorylation of tyrosine residues in this region leads to a conformation change and activation of the kinase.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Tissue specificity: Expressed in bone marrow and in differentiated blood mononuclear cells.
Induction: Up-regulated by glucocorticoids.
Post-translational: Autophosphorylated in response to CSF1 or IL34 binding. Phosphorylation at Tyr-561 is important for normal down-regulation of signaling by ubiquitination, internalization and degradation. Phosphorylation at Tyr-561 and Tyr-809 is important for interaction with SRC family members, including FYN, YES1 and SRC, and for subsequent activation of these protein kinases. Phosphorylation at Tyr-699 and Tyr-923 is important for interaction with GRB2. Phosphorylation at Tyr-723 is important for interaction with PIK3R1. Phosphorylation at Tyr-708 is important for normal receptor degradation. Phosphorylation at Tyr-723 and Tyr-809 is important for interaction with PLCG2. Phosphorylation at Tyr-969 is important for interaction with CBL. Dephosphorylation by PTPN2 negatively regulates downstream signaling and macrophage differentiation.
Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation.
Involvement in disease: Note=Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.
Note=Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.
Leukoencephalopathy, diffuse hereditary, with spheroids (HDLS) [MIM:221820]: An autosomal dominant adult-onset rapidly progressive neurodegenerative disorder characterized by variable behavioral, cognitive, and motor changes. Patients often die of dementia within 6 years of onset. Brain imaging shows patchy abnormalities in the cerebral white matter, predominantly affecting the frontal and parietal lobes. Note=The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.
Contains 5 Ig-like C2-type (immunoglobulin-like) domains.
Contains 1 protein kinase domain.
General information above from UniProt

M-CSFR encoded by the proto-oncogene c-fms is the receptor for colony stimulating factor 1 (CSF1R), a cytokine involved in the proliferation, differentiation, and activation of macrophages. This cell surface glycoprotein is consisted by an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Binding of CSF1 activates the receptor kinase, leading to "autophosphorylation" of receptor subunits and the concomitant phosphorylation of a series of cellular proteins on tyrosine residues. CSF1R is a tyrosine kinase receptor that is absolutely required for macrophage differentiation and thus occupies a central role in hematopoiesis. CSF1 and its receptor (CSF1R, product of c-fms proto-oncogene) were initially implicated as essential for normal monocyte development as well as for trophoblastic implantation. This apparent role for CSF1/CSF1R in normal mammary gland development is very intriguing because this receptor/ligand pair has also been found to be important in the biology of breast cancer in which abnormal expression of CSF1 and its receptor correlates with tumor cell invasiveness and adverse clinical prognosis. Tumor cell expression of CSF1R is under the control of several steroid hormones (glucocorticoids and progestins) and the binding of several bHLH transcription factors, while tumor cell expression of CSF-1 appears to be regulated by other hormones, some of which are involved in normal lactogenic differentiation. However, studies have demonstrated that CSF1 and CSF1R have additional roles in mammary gland development during pregnancy and lactation. The role of CSF1 and CSF1R in normal and neoplastic mammary development that may elucidate potential relationships of growth factor-induced biological changes in the breast during pregnancy and tumor progression.

CSF1R/MCSF Receptor/CD115 Alternative Name

CSF1R/MCSF Receptor/CD115 Related Studies

  • Sherr CJ. (1990) The colony-stimulating factor 1 receptor: pleiotropy of signal-response coupling. Lymphokine Res. 9(4): 543-8.
  • Kacinski BM. (1997) CSF-1 and its receptor in breast carcinomas and neoplasms of the female reproductive tract. Mol Reprod Dev. 46(1): 71-4.
  • Sapi E, et al. (1999) The role of CSF-1 in normal and neoplastic breast physiology. Proc Soc Exp Biol Med. 220(1): 1-8.
  • Sapi E. (2004) The role of CSF-1 in normal physiology of mammary gland and breast cancer: an update. Exp Biol Med (Maywood). 229(1): 1-11.
  • Bonifer C, et al. (2008) The transcriptional regulation of the Colony-Stimulating Factor 1 Receptor (csf1r) gene during hematopoiesis. Front Biosci. 13: 549-60.
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