G-CSF Protein, Human

Granulocyte colony-stimulating factor (G-CSF) is a glycoprotein secreted by the cells of the immune system, fibroblasts and endothelium, which acts as a hematopoietic and endothelial precursor cells cytokine. G-CSF stimulates maturation of progenitor cells in the bone marrow into differentiated granulocytes, macrophages and the T cells. G-CSF also shows to convey neuroprotection to central neurons upon increases in phosphorylation of PI3K/Akt pathway and regulates epithelial to mesenchymal transition in cancer. G-CSF Protein (Human) is a recombinant protein with tag free that consists of 200 or 204 amino acids, which is expressed in E. coli^{[1][2][3][4][5][6][7][8]}.

G-CSF Protein (Human) is a glycoprotein, acting to stimulate granulopoiesis, the innate immunity, and the differentiation of neural progenitor cells^[1].
G-CSF Protein (Human) levels are associated with various cancers, such as lung cancer, glioma, colorectal cancers, bladder cancer, melanoma, skin carcinom, bone metastases in cancers of prostate and breast, , and more^[1].
G-CSF Protein (Human) acts via a specific cognate receptor (G-CSFR) that belongs to the class I cytokine receptor superfamily, and then activates members of the Janus kinase family (JAK1, JAK2, and TYK2), cytoplasmic tyrosine kinases associated with Box 1. G-CSF Protein (Human) stimulates the proliferation, differentiation, and function of myeloid progenitors and mobilization of hematopoietic stem and progenitor cells, which shows potential application for skeletal muscle repair and regeneration^[2].
G-CSF Protein (Human) induces hematopoietic stem/progenitor cell mobilisation and stimulates angiogenesisrelated endothelial cell proliferation and migration and has the potential to inhibit the progression of atherosclerosis in animal models^[3].
G-CSF Protein (Human) expression is enhanced by activation of the RAS/MEK/ERK pathway through the Ets transcription factor and promotes resistance to anti-VEGF therapy^[5].
G-CSF Protein (Human) promotes the viability and angiogenesis of injured liver via direct efects on the liver cells^[8].

Incubation of alpha-smooth muscle actin (αSMA⁺)/CD105⁺/CD31^- cells with FGFs induces G-CSF Protein (Human) release in a MEK-dependent manner^[5].
G-CSF Protein (Human) (0.5, 1, 10 μg/mL, 0-96 h) directly promotes cell viability and VEGF-A expression in human injured liver cells^[8].

G-CSF Protein (Human) improves recovery after muscle crush injury, significantly increasing muscle strength in male Wistar rats. G-CSF Protein (Human) also increases rates of regeneration and activation of anabolic signalling pathways, such as Akt in mice injected with snake venom to cause skeletal muscle necrosis^[2].
G-CSF Protein (Human) (≤100 μg/kg, i.v. or s.c. or i.p., daily for 6,8,12 weeks) reduces the area of atherosclerotic lesions in rabbit and mouse models of atherosclerosis^[3].
G-CSF Protein (Human) (5 μg/kg , infusion, a sinfle dose at 4 h and 24 h) induces a 3-4 fold spike in circulating endothelial progenitor cells (CEPs) levels, similar to that using OXi-4503 (HY-16147) in non tumor bearing BALB/c and C57Bl/6 mice^[4].
G-CSF Protein (Human) plasma levels are substantially elevated after treated with OXi-4503 (HY-16147) (100 mg/kg, i.p., a single dose for 4 h) in G-CSF-R^−/− mice bearing subcutaneous Lewis Lung Carcinoma (LLC) transplants^[4].
G-CSF Protein (Human)--mediated resistance to antivascular endothelial growth factor (VEGF) therapies occurs through activation of RAS/MEK/ERK pathways and an Ets-induced overexpression of G-CSF Protein (Human) in murine models of pancreatic adenocarcinoma expressing RAS oncogene^[5].
G-CSF Protein (Human) (250 µg/kg, s.c., a single dose) relieves liver injury and shows positive correlation with viability and angiogenesis in the injured liver in the injured liver mouse model^[8].

The ED₅₀ is <0.1 ng/mL as measured by M-NFS-60 cells, corresponding to a specific activity of >1.0 × 10⁷ units/mg.

• 
  Measured in a cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cells. The ED₅₀ for this effect is 10.17 pg/mL, corresponding to a specific activity is 9.83×10⁷ units/mg.

Human

E. coli

Tag Free

Q8N4W3 (T27-P200)/P09919-2 (T31-P204)

1440  [NCBI]

Full Length of Mature Protein

TPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLCATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP

Approximately 16 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 10 mM HAc-NaAc, 150 mM NaCl, 0.004% Tween 80, 5% Mannitol, pH 4.0.
2.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.
3.Lyophilized from a 0.22 μm filtered solution of 25 mM Tris, pH 8.0.
4.Lyophilized from a 0.22 μm filtered solution of 10 mM HAc-NaAc, 150 mM NaCl, pH 4.0.
5.Lyophilized from a 0.22 μm filtered solution of 10 mM HAc-NaAc, 150 mM NaCl, pH 4.0, 10% trehalose, 0.02% Tween80.
6.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Aliper AM, et al. A role for G-CSF and GM-CSF in nonmyeloid cancers. Cancer Med. 2014 Aug;3(4):737-46.  [Content Brief]

  [2]. Wright CR, et al. Granulocyte Colony-Stimulating Factor and Its Potential Application for Skeletal Muscle Repair and Regeneration. Mediators Inflamm. 2017;2017:7517350.  [Content Brief]

  [3]. Liu M, et al. The Effect of Granulocyte Colony-Stimulating Factor on the Progression of Atherosclerosis in Animal Models: A Meta-Analysis. Biomed Res Int. 2017;2017:6705363.  [Content Brief]

  [4]. Shaked Y, et al. Contribution of granulocyte colony-stimulating factor to the acute mobilization of endothelial precursor cells by vascular disrupting agents. Cancer Res. 2009 Oct 1;69(19):7524-8.  [Content Brief]

  [5]. Phan VT, et al. Oncogenic RAS pathway activation promotes resistance to anti-VEGF therapy through G-CSF-induced neutrophil recruitment. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):6079-84.  [Content Brief]

  [6]. Galván ST, et al. Plasma concentrations of granulocyte colony-stimulating factor (G-CSF) in patients with substance use disorders and comorbid major depressive disorder. Sci Rep. 2021 Jul 1;11(1):13629.  [Content Brief]

  [7]. Ding J, et al. M2 macrophage-derived G-CSF promotes trophoblasts EMT, invasion and migration via activating PI3K/Akt/Erk1/2 pathway to mediate normal pregnancy. J Cell Mol Med. 2021 Feb;25(4):2136-2147.  [Content Brief]

  [8]. Liu Z, et al. G-CSF promotes the viability and angiogenesis of injured liver via direct effects on the liver cells. Mol Biol Rep. 2022 Sep;49(9):8715-8725.  [Content Brief]