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G-CSF Protein

CSF3 Spezies: Human Wirt: Escherichia coli (E. coli) Recombinant > 98 % as determined by:(a) Analysis by SEC-HPLC(b)Analysis by reducing and non-reducing SDS-PAGE silver-stained gel Active
Produktnummer ABIN987880
  • Target Alle G-CSF (CSF3) Proteine anzeigen
    G-CSF (CSF3) (Colony Stimulating Factor 3 (Granulocyte) (CSF3))
    Protein-Typ
    Recombinant
    Biologische Aktivität
    Active
    Spezies
    • 29
    • 10
    • 4
    • 3
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    Human
    Quelle
    • 25
    • 11
    • 5
    • 3
    • 2
    • 2
    • 1
    • 1
    • 1
    Escherichia coli (E. coli)
    Sequenz
    analysis The sequence of the first fifteen N-terminal amino acids was determined and was found to be Met-Thr-Pro-Leu-Gly-Pro-Ala-Ser-Ser-Leu-Pro-Gln-Ser-Phe-Leu-Leu. p to grams level.
    Produktmerkmale
    The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to aof 6.0×107 IU/mg
    Reinheit
    > 98 % as determined by:(a) Analysis by SEC-HPLC(b)Analysis by reducing and non-reducing SDS-PAGE silver-stained gel
    Endotoxin-Niveau
    Level Less than 0.03ng/µg (0.3 IEU/µg) determined by LAL test
    Top Product
    Discover our top product CSF3 Protein
  • Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Lyophilized
    Rekonstitution
    It is recommended to reconstitute the lyophilized Recombinant Human Granulocyte Colony Stimulating Factor (G-CSF) in sterile 18 M-omega-cm H2O not less than 100 myg/ml, which can then be further diluted to other aqueous solutions. Quantitation Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.815 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a standard solution of recombinant G-CSF as a Reference Standard.
    Lagerung
    -20 °C
  • Xie, Gorodetsky, Micewicz, Micevicz, Mackenzie, Gaberman, Levdansky, McBride: "Marrow-derived stromal cell delivery on fibrin microbeads can correct radiation-induced wound-healing deficits." in: The Journal of investigative dermatology, Vol. 133, Issue 2, pp. 553-61, (2013) (PubMed).

  • Target
    G-CSF (CSF3) (Colony Stimulating Factor 3 (Granulocyte) (CSF3))
    Andere Bezeichnung
    Granulocyte Colony Stimulating Factor (G-CSF) (CSF3 Produkte)
    Synonyme
    CSF3 Protein, G-CSF Protein, gcsf Protein, Csfg Protein, MGI-IG Protein, C17orf33 Protein, CSF3OS Protein, GCSF Protein, Gcsf Protein, colony stimulating factor 3 Protein, colony stimulating factor 3 (granulocyte) a Protein, colony stimulating factor 3 (granulocyte) Protein, CSF3 Protein, csf3a Protein, Csf3 Protein
    Hintergrund
    Human Granulocyte Colony Stimulating Factor (G-CSF) contains internal disulfide bonds. Among the family of colony-stimulating factors, Granulocyte Colony Stimulating Factor (G-CSF) is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of Granulocyte Colony Stimulating Factor (G-CSF) can be induced by bacterial endotoxins, TNF, Interleukin-1 and GM-CSF. Prostaglandin E2 inhibits the synthesis of Granulocyte Colony Stimulating Factor (G-CSF). In epithelial, endothelial, and fibroblastic cells secretion of Granulocyte Colony Stimulating Factor (G-CSF) is induced by Interleukin-17. Recombinant Human Granulocyte Colony Stimulating Factor (G-CSF) produced in E. coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18,800 Da. Synonym: rHuG-CSF, G-CS. Formulation: The protein was lyophilized after extensive dialysis against 10mM HAc-NaAc, pH4.0, 150mM NaCl, 0.004% Tween 80, 5% Mannitol buffer.
    Molekulargewicht
    18,800 Da Isoelectric Point The main zone between 5.8-6.6 analysis by IEF UV Scan The maximal absorption wave is 278+/-3 nm.
    Pathways
    Cellular Response to Molecule of Bacterial Origin, Regulation of Actin Filament Polymerization
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