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
- Pack Size: 10 µgCentrifuge vial prior to reconstitution. Reconstitute to 500 μg/ml by adding 20 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.Pack Size: 100 µgCentrifuge 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
- 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.
- Guaranteed for 3 months from the date of reconstitution or until the date of expiry, whichever comes first. Please see label for expiry date.
- 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
- 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
- For research purposes only
Applications of G-CSF
|Application Name||Verified||Min Dilution||Max Dilution|
Useful Reagents Available
|Description||Product Code||Applications||Pack Size||List Price||Quantity|
|Rat anti Human G-CSF||1012701||E WB||0.5 mg|
|Rat anti Human G-CSF||1012801||E WB||0.5 mg|
|Rabbit anti Human G-CSF||AHP1031||E FN P* WB||0.1 mg|
|alamarBlue®||BUF012A||E FN IF||25 ml|
|Recombinant Human G-CSF||PHP082B||FN||10 µg|
Product Specific References
Avalos, B.R. (1996) Molecular analysis of the granulocyte colony-stimulating factor receptor.
Blood. 88 (3): 761-77.
Cavalcante, M.B. et al. (2015) Granulocyte colony-stimulating factor and reproductive medicine: A review.
Iran J Reprod Med. 13 (4): 195-202.
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.
Crawford, J. et al. (2004) Chemotherapy-induced neutropenia: risks, consequences, and new directions for its management.
Cancer. 100 (2): 228-37.
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.
Lustberg, M.B. (2012) Management of neutropenia in cancer patients.
Clin Adv Hematol Oncol. 10 (12): 825-6.
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.
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.