Detects human G‑CSF R/CD114 in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant human (rh) GM-CSF R alpha, rhGM-CSF R beta, or rhM-CSF R is observed.
Monoclonal Mouse IgG1 Clone # 38660
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human G‑CSF R/CD114 Glu25-Pro621 Accession # Q99062
Supplied in a saline solution containing BSA and Sodium Azide.
Detection of G‑CSF R/CD114 in Human Blood Granulocytes by Flow Cytometry.
Human peripheral blood granulocytes were stained with Mouse Anti-Human G‑CSF R/CD114 Fluorescein‑conjugated Monoclonal Antibody (Catalog # FAB381F, filled histogram) or isotype control antibody (Catalog # IC002F, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
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, also known as Colony-Stimulating Factor 3 Receptor (CSF3R) and designated CD114, 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).
Nicola, N.A., in Cytokine Reference, (2001) Oppenhiem, J.J. and M. Feldmann, eds. Academic Press p. 1935
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