• Species Reactivity

  Human

• Specificity

  Detects human G-CSF R/CD114 in ELISAs and Western blots. In sandwich Immunoassays, no cross-reactivity with recombinant human (rh) G‑CSF, rhGM‑CSF R beta, rhGM‑CSF R, or recombinant mouse G‑CSF is observed.

• Source

  Monoclonal Mouse IgG1 Clone # 38643

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant human G-CSF R/CD114    
  Glu25-Pro621    
  Accession # Q99062

• Formulation

  Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

• Label

  Alexa Fluor 405

Applications

• Recommended    
  Concentration

  Sample

• Flow Cytometry

  0.25-1 µg/10    ⁶ cells

  Human whole blood monocytes and human whole blood granulocytes

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Preparation and Storage

• Shipping

  The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

• Stability & Storage

  Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Background: G-CSF R/CD114

Granulocyte Colony Stimulating Factor (G-CSF) is a pleiotropic cytokine best known for its specific effects on the proliferation, differentiation, and activation of hematopoietic cells of the neutrophilic granulocyte lineage. G-CSF plays an important role in defense against infection, in inflammation and repair, and in the maintenance of steady state hematopoiesis. Recombinant human G-CSF has been approved for the amelioration of chemotherapy induced neutropenia as well as for severe chronic neutropenia following marrow transplant. Cell activation by G-CSF is mediated by a type I membrane protein belonging to the cytokine receptor superfamily. Human G-CSF R is 863 amino acids (aa) in length, with a 604 aa extracellular domain, a 26 aa transmembrane domain, and a 183 aa cytoplasmic domain that include a 23 amino acid signal sequence. As a result of alternative splicing, at least four isoforms of G-CSF R that differ in their C-terminal region exist. Isoform 2 lacks the transmembrane region and may represent a soluble form of the receptor; however the existence of soluble G-CSF R in human serum has not been reported (1). Mutations have been found in the gene encoding G-CSF R in some patients with severe congenital neutropenia. These mutations typically led to a truncation in the cytoplasmic domain of the G-CSF R leading to maturation arrest of neutrophil precursors in the bone marrow and neutropenia in peripheral blood (2). Human and mouse G-CSF R have a homology of 62.5%. G-CSF R is expressed in mature neutrophils, neutrophilic precursors, myeloid leukemia cells, and placenta. Binding of G-CSF to its receptor induces dimerization or oligomerization of the receptor activating cytoplasmic tyrosine kinases. Signal transduction from pathways that involve Janus tyrosine kinases/signal transducer and activator of transcription proteins (Jak1, Jak2, and Tyk2/STAT3, STAT3, and STATG), src-related protein tyrosine kinases (Lyn and Syk), Ras/MAP kinase, and phosphatidylinositol have been reported to be activated upon G-CSF stimulation (1).

• References:

1. Nicola, N.A., in Cytokine Reference, (2001) Oppenhiem, J.J. and M. Feldmann, eds. Academic Press p. 1935

2. Mitsui, T. et al. (2003) Blood. 101:2990.

• Long Name:

  Granulocyte Colony Stimulating Factor Receptor

• Entrez Gene IDs:

  1441 (Human); 12986 (Mouse)

• Alternate Names:

  CD114 antigen; CD114; colony stimulating factor 3 receptor (granulocyte); CSF3R; Csfgr; G-CSF R; G-CSF receptor; GCSFR; G-CSFR; GCSFRG-CSF-R; granulocyte colony-stimulating factor receptor