|Detection of Human G‑CSF R/CD114 by Western Blot. Western blot shows lysates of AML‑193 human acute monocytic leukemia cell line. PVDF membrane was probed with 0.5 µg/mL of Goat Anti-Human G‑CSF R/CD114 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-381-PB) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for G‑CSF R/CD114 at approximately 145 kDa (as indicated). This experiment was conducted under reducing conditions using Immunoblot Buffer Group 1.|
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).
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