G-CSF Protein, Human

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Based on 2 publication(s) in Google Scholar

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.

For research use only. We do not sell to patients.
  • Species: Human
  • Source: E. coli
  • Storage:
    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.
  • Biological Activity
  • Technical Parameters
  • Product Properties
  • Documentation
  • References
  • Help & FAQs

Biological Activity

Description

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].

Background

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].

In Vitro

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].

In Vivo

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].

Verified Bioactivity

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.

Results
  • Experimental Validation Results for G-CSF Protein, Human
    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.

Technical Parameters

  • Species Human
  • Source E. coli
  • Tag Tag Free
  • Accession
  • Gene ID
  • Molecular Construction
    • N-term
    • G-CSF (T31-P204)
      Accession # P09919-2
    • C-term
  • Protein Length

    Full Length of Mature Protein

  • Synonyms

    Granulocyte Colony-Stimulating Factor; G-CSF; Pluripoietin; Filgrastim; Lenograstim; CSF3; C17orf33; GCSF

  • AA Sequence

    TPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLCATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP

  • Predicted Molecular Mass

    18.8 kDa

  • Molecular Weight

    Approximately 16-19 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

  • Purity

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

    • Experimental Validation Results for G-CSF Protein, Human
      ≥ 95%, as determined by reducing SDS-PAGE.

Product Properties

Appearance

Lyophilized powder

Formulation

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.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

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).

Storage & Stability

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.

Shipping

Room temperature in continental US; may vary elsewhere.

References

[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]

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Calculators

Reconstitution Calculator

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Dilution Calculator

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The Specific Activity Calculator Equation
  • Specific Activity (Unit/mg)
  • Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) Specific Activity (Unit/mg)
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Biological Activity (ED50) Biological Activity (ED50)
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MOQ
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100 mg

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