Render Target: STATIC
Render Timestamp: 2024-11-01T09:46:12.568Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-10-11 20:01:07.043
Product last modified at: 2024-10-12T07:00:54.680Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

CSF-1R/M-CSF-R (E7S2S) Rabbit mAb #14582

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 175
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Simple Western™ 1:10 - 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    CSF-1R/M-CSF-R (E7S2S) Rabbit mAb recognizes endogenous levels of total CSF-1R/M-CSF-R protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly92 of human CSF-1R/M-CSF-R protein.

    Background

    Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation, and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).

    After initial dimerization and autophosphorylation, the M-CSF receptor undergoes a regulated intramembrane proteolysis (RIP) involving two cleavage events. Extracellular cleavage of this membrane protein results in release of the extracellular domain, while cleavage in the transmembrane region releases the cytoplasmic domain into the cytosol (9). The activated intracellular domain localizes to the nucleus to regulate transcription of specific pro-inflammatory genes (10). Research studies indicate that the processing and down regulation of M-CSF receptor is a continuous process whose rate increases in response to various stimuli, including PMA, LPS, tumor necrosis factor, IL-2, Il-4, and the physiological ligand M-CSF (9).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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