Conditions of optimal G-CSF protein performance should be determined experimentally by the investigator.
Human Granulocyte-Colony-Stimulating Factor (G-CSF), a 20 kDa glycoprotein containing internal disulfide bonds, induces the survival, proliferation, and differentiation of neutrophilic granulocyte precursor cells and functionally activates mature blood neutrophils. G-CSF functions through the Janus kinase (JAK)/signal transducer and activator of transcription (STAT), Ras/mitogen-activated protein kinase (MAPK), and phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt) signal transduction pathway. Among the family of colony-stimulating factors, G-CSF is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. Bacterial endotoxins, TNF, Interleukin-1, and GM-CSF induce the synthesis of G-CSF while prostaglandin E2 inhibits its synthesis. Interleukin-17 induces the secretion of G-CSF in epithelial, endothelial, and fibroblastic cells.
BP000175-GD16: Recombinant Human Granulocyte colony-stimulating factor (G-CSF) Protein
Source: E. coli-derived.
N-terminal sequence analysis: Met-Thr-Pro-Leu-Gly-Pro-Ala-Ser-Ser-Leu-Pro-Gln-Ser- Phe-Leu-leu.
Predicted molecular mass: 20 kDa, the 174-amino acid form of human G-CSF.
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells is < 0.1 ng/ml, corresponding to a specific activity of 6.0x10^7 IU/mg.
Purity: > 95% by SEC-HPLC and reducing SDS-PAGE.
Endotoxin: < 0.01 ng/ug (0.1 IEU/ug).
Formulation: In 0.2 um filtered solution of 10 mM HAc-NaAc, 150 mM NaCl, 0.004% Tween 80, 5% Mannitol, pH 4.0.
Shipping: The product is shipped at 4°C. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt if stored at 4°C as supplied.
Other G-CSF Proteins:
Recombinant human Pegylated G-CSF protein
Recombinant human G-CSF protein with His-tag
Recombinant human G-CSF protein produced in HEK
Recombinant human G-CSF protein produced in CHO
Recombinant mouse G-CSF protein
There are two forms, 174- and 180-amino-acid, of the natural human G-CSF protein. The 174-amino acid form is more abundant and active than the longer form and widely used in research and therapeutics. The structure of the recombinant human G-CSF protein expressed in E. coli, such as filgrastim, differs slightly from those of the natural glycoprotein and the recombinant human G-CSF protein expressed in mammalian cells such as CHO cells. PEGylation (polyethylene glycol) significantly extends half-life of the recombinant human G-CSF protein.