Recombinant human G-CSF protein
QK074
Brand: Qkine
Granulocyte colony-stimulating factor (G-CSF) is a member of the hematopoietic growth factor family which plays a crucial role in the proliferation, differentiation, and maturation of committed progenitor cells to granulocytes, such as neutrophils.
Qkine G-CSF is a highly pure, bioactive glycoprotein produced in an animal origin-free expression system composed of 174 amino acids with a molecular weight of 18.6 kDa. Human and murine G-CSF are 73% identical at the amino acid level and show species cross-reactivity. Human G-CSF is carrier-free, tag-free, and non-glycosylated to ensure a pure and homogenous production of high-quality neutrophils and other relevant cell cultures with exceptional lot-to-lot consistency.

Currency:
Product name | Catalog number | Pack size | Price | Price (USD) | Price (GBP) | Price (EUR) |
---|---|---|---|---|---|---|
Recombinant human G-CSF protein, 25 µg | QK074-0025 | 25 µg | (select above) | $ 280.00 | £ 205.00 | € 240.00 |
Recombinant human G-CSF protein, 50 µg | QK074-0050 | 50 µg | (select above) | $ 410.00 | £ 305.00 | € 357.00 |
Recombinant human G-CSF protein, 100 µg | QK074-0100 | 100 µg | (select above) | $ 620.00 | £ 455.00 | € 532.00 |
Recombinant human G-CSF protein, 500 µg | QK074-0500 | 500 µg | (select above) | $ 2,500.00 | £ 1,840.00 | € 2,150.00 |
Recombinant human G-CSF protein, 1000 µg | QK074-1000 | 1000 µg | (select above) | $ 3,950.00 | £ 2,900.00 | € 3,388.00 |
Note: prices shown do not include shipping and handling charges.
Qkine company name and logo are the property of Qkine Ltd. UK.
Alternative protein names
Species reactivity
human
species similarity:
mouse – 75%
rat – 73%
porcine – 79%
bovine – 81%
Frequently used together:
Summary
- High purity human G-CSF protein (Uniprot: P09919-2)
- 18.6 kDa (monomer)
- >98%, by SDS-PAGE quantitative densitometry
- Expressed in E. coli
- Animal origin-free (AOF) and carrier protein-free
- Manufactured in Qkine's Cambridge, UK laboratories
- Lyophilized from Tris, mannitol
- Resuspend in sterile-filtered water at >50 µg/ml, add carrier protein if desired, prepare single use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term).
Featured applications
- Generation of iPSC-derived neutrophils
- Induction of cardiomyocytes from iPSCs
- Mobilization of bone marrow cells for wound healing applications
- Regulation of ZO-1 expression in brain microvascular endothelial cells
- Proliferation of neutrophils
- Maintenance of isolated neutrophils
Bioactivity
Purity
Further quality assays
- Mass spectrometry, single species with the expected mass
- Endotoxin: <0.005 EU/μg protein (below the level of detection)
- Recovery from stock vial: >95%
Qkine G-CSF was as biologically active as a comparable supplier protein. G-CSF activity was determined using the Promega CellTiter-Glo luminescent cell viability assay. NFS-60 mouse myeloid leukemia cells were treated in triplicate with a serial dilution of Qkine G-CSF (Qk074, green) or an alternative supplier G-CSF (Supplier B, black) for 48 hours. Cell viability was measured and normalized. Data from Qk074 lot #204487.
Protein background
Granulocyte colony-stimulating factor (G-CSF), or colony-stimulating factor 3 (CSF-3), is a secreted glycoprotein belonging to the family of hematopoietic growth factors. It regulates granulopoiesis leading to the maturation of committed progenitors to granulocytes, such as neutrophils [1–3]. G-CSF is involved in the proliferation, maturation, and mobilization of neutrophils in both the healthy and diseased states [3,4]. It was one of the first cytokines to be identified in vitro and was successfully isolated from human cells in 1984 [4–7].
Human G-CSF is composed of 174 amino acids with a molecular weight of 18.6 kDa [3]. G-CSF can be released by various cells such as macrophages, fibroblasts, endothelial cells, and epithelial cells [4] under inflammatory mediators’ stimulation such as interleukin (IL)-17 and IL-1, tumor necrosis factor (TNF)-α, interferon (IFN)-β, lipopolysaccharide (LPS) as well as vascular endothelial growth factor (VEGF) [8–10].
G-CSF binds to the homodimer GCSF receptor (GCSF-R) expressed on myeloid cells as well as fibroblasts, endothelial cells, and bone marrow stromal cells [2,11]. GCSF-R is an 813-amino acid protein and is composed of an extracellular region, which consists of an immunoglobin-like domain, a cytokine receptor homologous domain, three fibronectin type III-like domains, a transmembrane region, and an intracellular region [1]. G-CSF binds to G-CSFR, resulting in its dimerization and the activation of downstream signaling pathways. Among the activated downstream signal transduction pathways are Janus kinase (JAK)/signal transducer and activator of transcription (STAT), Src kinases such as Lyn, Ras/Extracellular Regulated Kinase (ERK), and phosphatidylinositol 3-kinase (PI3K).
G-CSF has been used in vitro to maintain neutrophils and stimulate the differentiation of cells to neutrophil lineage [12] such as generating functional neutrophils from iPSCs [13,14]. In addition, G-CSFR was shown to contribute to the activation of STAT signaling and cardiac differentiation from iPSCs [15].
G-CSF has been shown to have aberrant expression in some disorders such as Alzheimer’s disease. A study by Zhang et al. reported that G-CSF downregulates ZO-1 expression in brain microvascular endothelial cells highlighting a potential therapeutic target for Alzheimer’s disease [16].
In vivo, G-CSF was shown to contribute to the improvement of memory and neurobehavioral function in an amyloid-beta-induced experimental model of Alzheimer’s disease [17]. In wound healing applications, G-CSF has been shown to have a crucial role in mobilizing bone marrow-derived cells to accelerate the wound healing process [18]. Hence, it is administered following bone marrow transplantation to facilitate hematopoietic recovery. Finally, G-CSF is used as a therapeutic agent in neutropenia, a condition resulting in a low number of neutrophils in the blood, particularly in patients with cancer undergoing chemotherapy [4,19].
Background references
- Park SD, Saunders AS, Reidy MA, Bender DE, Clifton S, Morris KT. A review of granulocyte colony-stimulating factor receptor signaling and regulation with implications for cancer. Front Oncol. 2022 Aug 11;12:4042.
- Link H. Current state and future opportunities in granulocyte colony-stimulating factor (G-CSF). Supportive Care in Cancer. 2022 Sep 1;30(9):7067–77.
- Karagiannidis I, Salataj E, Said Abu Egal E, Beswick EJ. G-CSF in tumors: aggressiveness, tumor microenvironment and immune cell regulation. Cytokine. 2021 Jun 1;142:155479.
- Bendall LJ, Bradstock KF. G-CSF: From granulopoietic stimulant to bone marrow stem cell mobilizing agent. Cytokine Growth Factor Rev. 2014 Aug 1;25(4):355–67.
- Bradley TR, Metcalf D. THE GROWTH OF MOUSE BONE MARROW CELLS IN VITRO. Australian Journal of Experimental Biology and Medical Science. 1966 Jun 1;44(3):287–300.
- Ichikawa Y, Pluznik DH, Sachs L. In vitro control of the development of macrophage and granulocyte colonies. Proc Natl Acad Sci U S A [Internet]. 1966 Aug 1 [cited 2023 Apr 24];56(2):488–95. Available from: https://www.pnas.org/doi/abs/10.1073/pnas.56.2.488
- Welte K, Platzer E, Lu L, Gabrilove JL, Levi E, Mertelsmann R, et al. Purification and biochemical characterization of human pluripotent hematopoietic colony-stimulating factor. Proceedings of the National Academy of Sciences. 1985 Mar 1;82(5):1526–30.
- Nicola NA. Granulocyte colony-stimulating factor. Immunol Ser. 1990 Jan 1;49:77–109.
- Fossiez F, Djossou O, Chomarat P, Flores-Romo L, Ait-Yahia S, Maat C, et al. T cell interleukin-17 induces stromal cells to produce proinflammatory and hematopoietic cytokines. Journal of Experimental Medicine. 1996 Jun 1;183(6):2593–603.
- Sano E, Ohashi K, Sato Y, Kashiwagi M, Joguchi A, Naruse N. A possible role of autogenous IFN-β for cytokine productions in human fibroblasts. J Cell Biochem. 2007 Apr 15;100(6):1459–76.
- Demetri G, Griffin J. Granulocyte Colony-Stimulating Factor and Its Receptor. Blood. 1991 Dec 1;78(11):2791–808.
- Panopoulos AD, Watowich SS. Granulocyte colony-stimulating factor: molecular mechanisms of action during steady state and ‘emergency’ hematopoiesis. Cytokine. 2008 Jun;42(3):277.
- Brok-Volchanskaya VS, Bennin DA, Suknuntha K, Klemm LC, Huttenlocher A, Slukvin I. Effective and Rapid Generation of Functional Neutrophils from Induced Pluripotent Stem Cells Using ETV2-Modified mRNA. Stem Cell Reports [Internet]. 2019 Dec 12 [cited 2023 Apr 28];13(6):1099. Available from: /pmc/articles/PMC6915846/
- Majumder A, Suknuntha K, Bennin D, Klemm L, Brok-Volchanskaya VS, Huttenlocher A, et al. Generation of Human Neutrophils from Induced Pluripotent Stem Cells in Chemically Defined Conditions Using ETV2 Modified mRNA. STAR Protoc [Internet]. 2020 Sep 9 [cited 2023 Apr 28];1(2). Available from: /pmc/articles/PMC7543976/
- Tsukamoto T, Sogo T, Ueyama T, Nakao S, Harada Y, Ihara D, et al. Chimeric G-CSF Receptor-Mediated STAT3 Activation Contributes to Efficient Induction of Cardiomyocytes from Mouse Induced Pluripotent Stem Cells. Biotechnol J [Internet]. 2020 Feb 1 [cited 2023 Apr 28];15(2). Available from: https://pubmed.ncbi.nlm.nih.gov/31469473/
- Zhang X, Wang L, Zhang H, Tu F, Qiang Y, Nie C. Decreased expression of ZO-1 is associated with tumor metastases in liver cancer. Oncol Lett [Internet]. 2019 Feb 1 [cited 2023 Apr 28];17(2):1859. Available from: /pmc/articles/PMC6341828/
- Prakash A, Medhi B, Chopra K. Granulocyte colony stimulating factor (GCSF) improves memory and neurobehavior in an amyloid-β induced experimental model of Alzheimer’s disease. Pharmacol Biochem Behav [Internet]. 2013 [cited 2023 Apr 28];110:46–57. Available from: https://pubmed.ncbi.nlm.nih.gov/23756182/
- Wang Y, Sun Y, Yang XY, Ji SZ, Han S, Xia ZF. Mobilised bone marrow-derived cells accelerate wound healing. Int Wound J [Internet]. 2013 Aug 1 [cited 2023 Apr 28];10(4):473–9. Available from: https://onlinelibrary.wiley.com/doi/full/10.1111/j.1742-481X.2012.01007.x
- Cooper KL, Madan J, Whyte S, Stevenson MD, Akehurst RL. Granulocyte colony-stimulating factors for febrile neutropenia prophylaxis following chemotherapy: Systematic review and meta-analysis. BMC Cancer [Internet]. 2011 Sep 23 [cited 2023 Apr 26];11(1):1–11. Available from: https://bmccancer.biomedcentral.com/articles/10.1186/1471-2407-11-404