G-CSF Protein, Human, Recombinant (Fc Tag)


G-CSF Protein, Human, Recombinant (Fc Tag): Product Information

> 97 % as determined by SDS-PAGE
< 1.0 EU per μg of the protein as determined by the LAL method
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.
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.
Expressed Host
HEK293 Cells
Predicted N Terminal
Glu 20
Molecule Mass
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.
Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

G-CSF Protein, Human, Recombinant (Fc Tag): Images

G-CSF Protein, Human, Recombinant (Fc Tag): Alternative Names

C17orf33 Protein, Human; C17orf33OS Protein, Human; CSF3OS Protein, Human; G-CSF Protein, Human; GCSF Protein, Human

G-CSF Background Information

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.
Full Name
colony stimulating factor 3 (granulocyte)
  • 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.
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