Granulocyte colony stimulating factor (G-CSF or CSF-3) Price
BACKGROUND: Human graunlocyte colony stimulating factor (G-CSF or CSF-3) is a potent multi-functional growth factor/cytokine produced by
endothelial cells, fibroblasts, and immune cells. It is capable of mobilizing bone marrow hematopoietic stem cells, promoting growth and
differentiation of neutrophils, and inducing neurogenesis. These actions involve interaction with its specific membrane receptor, causing activation
of multiple signaling complexes such as JAK/STAT3, ERK, and AKT. The gene is located on chromosome 17, and produces five splice variants.
The longest splice form encodes a 30-amino acid signal peptide and 177-amino acid mature peptide. Clinically, G-CSF (Filgrastim or Neupogen)
is used to facilitate recovery from neutropenia after chemotherapy. Neulasta is pegylated G-CSF possessing prolonged in vivo stability. Unlike
growth hormone, G-CSF is not species specific. Although the protein is glycosylated, glycosylation is apparently not essential for its functions. The
human G-CSF is over-produced and purified from E. coli. The product is for research use only.
BACKGROUND: Human graunlocyte colony stimulating factor (G-CSF or CSF-3) is a potent multi-functional growth factor/cytokine produced by
endothelial cells, fibroblasts, and immune cells. It is capable of mobilizing bone marrow hematopoietic stem cells, promoting growth and
differentiation of neutrophils, and inducing neurogenesis. These actions involve interaction with its specific membrane receptor, causing activation
of multiple signaling complexes such as JAK/STAT3, ERK, and AKT. The gene is located on chromosome 17, and produces five splice variants.
The longest splice form encodes a 30-amino acid signal peptide and 177-amino acid mature peptide. Clinically, G-CSF (Filgrastim or Neupogen)
is used to facilitate recovery from neutropenia after chemotherapy. Neulasta is pegylated G-CSF possessing prolonged in vivo stability. Unlike
growth hormone, G-CSF is not species specific. Although the protein is glycosylated, glycosylation is apparently not essential for its functions. The
human G-CSF is over-produced and purified from E. coli. The product is for research use only.
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Biomedical Research Service
& Clinical Application
& Clinical Application
Human G-CSF activity is assessed by its ability to
stimulate the JAK/STAT3 signaling transduction
pathway. G-CSF at the indicated concentrations
was added to M-NSF-60 cells for 30 min in the
absence of serum. Cells were then harvested and
analyzed by Western blotting using rabbit
antibodies directed against phospho-STAT3
(Tyr705) and STAT3.
stimulate the JAK/STAT3 signaling transduction
pathway. G-CSF at the indicated concentrations
was added to M-NSF-60 cells for 30 min in the
absence of serum. Cells were then harvested and
analyzed by Western blotting using rabbit
antibodies directed against phospho-STAT3
(Tyr705) and STAT3.