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Human G-CSF / CSF3 Protein (Fc Tag)

C17orf33,C17orf33OS,CSF3OS,G-CSF,GCSF

Catalog Number P10007-H01H
Organism Species Human
Host Human Cells
Synonyms C17orf33,C17orf33OS,CSF3OS,G-CSF,GCSF
Molecular Weight The recombinant mature human GCSFb/Fc chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 412 amino acids and has a calculated molecular mass of 45.4 kDa. As a result of glycosylation, the rh GCSFb/Fc monomer migrates as an approximately 48 kDa protein in SDS-PAGE under reducing conditions.
predicted N Glu 20
SDS-PAGE
Purity > 97 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of human GCSF isoform b (NP_757373.1) (Ala 30-Pro 204) was fused with the Fc region of human IgG1 at the N-terminus.
Bio-activity Measured in a cell proliferation assay using a murine myeloblastic cell line, NFS-60. The ED50 for this effect is typically 0.2-0.8 ng/ml.
Research Area Cancer |Invasion microenvironment |Angiogenesis |Angiogenesis Growth Factor & Receptor
Formulation Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Granulocyte-colony stimulating factor (G-CSF) is a growth factor and an essential cytokine belonging to the CSF family of hormone-like glycoproteins. It is produced by numerous cell types including immune and endothelial cells. G-CSF binding to its receptor G-CSF-R which belongs to the cytokine receptor type I family depends on the interaction of alpha-helical motifs of the former and two fibronectin type III as well as an immunoglobulin-like domain of the latter. Recent animal studies have also revealed that G-CSF activates multiple signaling pathways, such as Akt and also the Janus family kinase-2 and signal transducer and activation of transcription-3 (Jak2-STAT3) pathway, thereby promoting survival, proliferation, differentiation and mobilisation of haematopoietic stem and progenitor cells. G-CSF is a cytokine that have been demonstrated to improve cardiac function and perfusion in myocardial infarction. And it was initially evaluated as a stem cell mobilizer and erythropoietin as a cytoprotective agent. G-CSF prevents left ventricular remodeling after myocardial infarction by decreasing cardiomyocyte death and by increasing the number of blood vessels, suggesting the importance of direct actions of G-CSF on the myocardium rather than through mobilization and differentiation of stem cells. Accordingly, recombinant human (rh)G-CSF has been extensively used in clinical haematology and oncology to enable bone marrow transplantation or to treat chemotherapy-associated neutropenia. In preclinical study, G-CSF improved cardiac function and perfusion by angiomyogenesis and protection of cardiomyocytes in myocardial infarction.
Reference
  • Takano H, et al. (2007) G-CSF therapy for acute myocardial infarction. Trends Pharmacol Sci. 28(10): 512-7.
  • Klocke R, et al. (2008) Granulocyte colony-stimulating factor (G-CSF) for cardio- and cerebrovascular regenerative applications. Curr Med Chem. 15(10): 968-77.
  • Kang HJ, et al. (2008) G-CSF- and erythropoietin-based cell therapy: a promising strategy for angiomyogenesis in myocardial infarction. Expert Rev Cardiovasc Ther. 6(5): 703-13.
  • Beekman R, et al. (2010) G-CSF and its receptor in myeloid malignancy. Blood. 115(25): 5131-6.