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SDS Safety Datasheet SDS
FN 100 µg loader
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Recombinant Human G-CSF
Granulocyte colony stimulating factor (G-CSF) is a member of the colony-stimulating factor hematopoietic cytokine family (Cavalcante et al. 2015). Similar to other cytokines, G-CSF plays a critical role in the immune response to infection. G-CSF is expressed by a number of cell types including monocytes, macrophages and fibroblasts (Panopoulos and Watowich 2008).

Protein levels are low in healthy individuals however increase significantly upon inflammatory stimuli such as interleukin 1 and TNF-alpha (Christensen et al. 2016, Panopoulos and Watowich 2008). G-CSF regulates neutrophilic granulocytes by stimulating neutrophil proliferation, differentiation, survival and also plays a key role in neutrophil mobilization into the bloodstream (Cavalcante et al. 2015).

G-CSF signaling is mediated by binding to the G-CSF receptor (G-CSFR, CD114 in humans), which is expressed by a number of cell types including myeloid leukemic cells, mature neutrophils, platelets, monocytes and cardiomyocytes (Panopoulos and Watowich 2008). Upon ligand binding, G-CSFR dimerizes, which results in receptor phosphorylation and subsequent activation of a number of cell signaling pathways, including JAK/STAT and Ras-MAPK signaling pathways (Tamada et al. 2005, Avalos 1996).

As a result of chemotherapy, cancer patients commonly develop neutropenia (Crawford et al. 2004). G-CSF is the active ingredient of drugs used to treat chemotherapy associated neutropenia (Lustberg 2012). G-CSF exacerbates inflammatory conditions such as rheumatoid arthritis; Eyles et al. (2008) suggest modulation of G-CSF as a potential therapy route.

The proliferative effect of G-CSF was demonstrated by performing a cell proliferation assay with NFS‑60 mouse myelogenous leukemia lymphoblast cells. The expected ED50 for this effect is 10-70 pg/ml.

Target Species
Product Form
Purified recombinant protein - lyophilized
Centrifuge vial prior to reconstitution. Reconstitute to 500 µg/ml by adding 200 μl ddH2O.
Care should be taken during reconstitution as the protein may appear as a film at the bottom of the vial. Bio-Rad recommend that the vial is gently mixed after reconstitution. Do not vortex.
Recombinant protein expressed in E.coli and purified by ion exchange chromatography
Buffer Solution
20 mM Phosphate Buffer, 0.1 M Sodium Chloride
Preservative Stabilisers
1.0% Trehalose
Confirmed by performing an alamarBlue® based cell proliferation assay using mouse myelogenous leukemia lymphoblast cells. The expected ED50 for this effect is 10-70 pg/ml.
≥98% determined by silver staining of SDS-PAGE gel
Approx. Protein Concentrations
500 μg/ml after reconstitution
Protein Molecular Weight
18.7 kDa
Endotoxin Level
< 1.0 EU/ug
For research purposes only
Guaranteed for 3 months from the date of reconstitution or until the date of expiry, whichever comes first. Please see label for expiry date.
alamarBlue is a trademark of Trek Diagnostic Systems, Inc and is manufactured for Bio-Rad by Trek Diagnostic Systems. U.S. patent 5,501,959

Prior to reconstitution store at -20oC. Following reconstitution store at -20oC.

This product should be stored undiluted.

Storage in frost-free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the protein. Should this product contain a precipitate we recommend microcentrifugation before use.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
Functional Assays
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.

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Further Reading

  1. Avalos, B.R. (1996) Molecular analysis of the granulocyte colony-stimulating factor receptor.
    Blood. 88 (3): 761-77.
  2. Cavalcante, M.B. et al. (2015) Granulocyte colony-stimulating factor and reproductive medicine: A review.
    Iran J Reprod Med. 13 (4): 195-202.
  3. Christensen, A.D. et al. (2016) Granulocyte colony-stimulating factor (G-CSF) plays an important role in immune complex-mediated arthritis.
    Eur J Immunol. 46 (5): 1235-45.
  4. Crawford, J. et al. (2004) Chemotherapy-induced neutropenia: risks, consequences, and new directions for its management.
    Cancer. 100 (2): 228-37.
  5. Eyles, J.L. et al. (2008) A key role for G-CSF-induced neutrophil production and trafficking during inflammatory arthritis.
    Blood. 112 (13): 5193-201.
  6. Lustberg, M.B. (2012) Management of neutropenia in cancer patients.
    Clin Adv Hematol Oncol. 10 (12): 825-6.
  7. Panopoulos, A.D. & Watowich, S.S. (2008) Granulocyte colony-stimulating factor: molecular mechanisms of action during steady state and 'emergency' hematopoiesis.
    Cytokine. 42 (3): 277-88.
  8. Tamada, T. et al. (2006) Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.
    Proc Natl Acad Sci U S A. 103 (9): 3135-40.
  9. View The Latest Product References

Entrez Gene
GO Terms
GO:0005125 cytokine activity
GO:0005130 granulocyte colony-stimulating factor receptor binding
GO:0005615 extracellular space
GO:0006955 immune response
GO:0008083 growth factor activity
GO:0008284 positive regulation of cell proliferation
GO:0019899 enzyme binding
GO:0019221 cytokine-mediated signaling pathway
GO:0030851 granulocyte differentiation


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