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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.

Qkine 3-for-2 product campaign

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
Granulocyte colony-stimulating factor, G-CSF, GCSF, GM-CSF beta, Colony-stimulating factor 3, CSF3, CSF-3, CSF3OS, Pluripoietin, Filgratin, Lenogratin, C17orf33, chromosome 17 open reading frame 33, MGC45931
Species reactivity

human

species similarity:
mouse – 75%
rat – 73%
porcine – 79%
bovine – 81%

Frequently used together with:

Summary

  • High purity human G-CSF protein (Uniprot: P09919-2)
  • >98%, by SDS-PAGE quantitative densitometry
  • Expressed in E. coli
  • 18.6 kDa monomer
  • Animal origin-free (AOF) and carrier protein-free
  • Manufactured in Cambridge, UK
  • Lyophilized from Tris/mannitol
  • Resuspend in water at >100 µg/ml, prepare single-use aliquots, add carrier protein if desired, and store frozen at -20°C or -80°C
Handling and Storage FAQ

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

Bioactivity graph showing the EC50 of 92 pg/ml (4.9 pM) for Qkine recombinant human G-CSF

G-CSF activity is determined using the Promega CellTiter-Glo luminescent cell viability assay. EC50 = 92 pg/ml (4.9 pM). NFS-60 mouse myeloid leukemia cells are treated in triplicate with a serial dilution of G-CSF for 48 hours. Cell viability is measured and normalized. Data from Qk074 lot #204487.

Purity

SDS-PAGE gel showing the high purity reduced and non-reduced forms of G-CSF

Recombinant G-CSF migrates as a major band at approximately 18 kDa (monomer) in non-reducing (NR) conditions.The dimeric form is the minor band at the higher molecular weight (36 kDa). Upon reduction (R), only the 18 kDa band is visible. No contaminating protein bands are present. The purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk074 batch #204487.

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%

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

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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
  7. 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.
  8. Nicola NA. Granulocyte colony-stimulating factor. Immunol Ser. 1990 Jan 1;49:77–109.
  9. 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.
  10. 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.
  11. Demetri G, Griffin J. Granulocyte Colony-Stimulating Factor and Its Receptor. Blood. 1991 Dec 1;78(11):2791–808.
  12. Panopoulos AD, Watowich SS. Granulocyte colony-stimulating factor: molecular mechanisms of action during steady state and ‘emergency’ hematopoiesis. Cytokine. 2008 Jun;42(3):277.
  13. 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/
  14. 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/
  15. 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/
  16. 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/
  17. 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/
  18. 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
  19. 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