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G-CSF Recombinant Protein
G-CSF Recombinant Protein

G-CSF Recombinant Protein

CATALOG NUMBER: 96-785
  • Tested Applications: ELISA, WB
  • Size: 0.05 mg

Specifications

  • SPECIES: Human
  • SOURCE SPECIES: HEK293 cells
  • RECOMBINANT PROTEIN SEQUENCE: Thr 31 - Pro 204
  • FUSION TAG: Tag Free
  • TESTED APPLICATIONS: ELISA, WB
  • APPLICATION NOTE: This recombinant protein can be used for E, WB. For research use only.
  • PREDICTED MOLECULAR WEIGHT: 18.7 kDa
  • BIOLOGICAL ACTIVITY: Measured by its binding ability in a functional ELISA. Immobilized Human G-CSF, Tag Free at 2 ug/mL (100 uL/well) can bind Biotinylated Human G-CSF R, His Tag with a linear range of 0.156-1.25 ug/mL.

Properties

  • PURITY: >95% as determined by SDS-PAGE.

    Endotoxin level is less than 1.0 EU per ug by the LAL method.
  • PHYSICAL STATE: Lyophilized
  • BUFFER: PBS, pH7.4
  • STORAGE CONDITIONS: Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles.

Additional Info

  • NCBI OFFICIAL SYMBOL: G-CSF
  • ADDITIONAL NAMES: G-CSF,CSF3,C17orf33,CSF3OS,MGC45931
  • Protein Accession Number: NP_757373.1
  • NCBI GENE ID NUMBER: 1440

Background

  • Granulocyte colony-stimulating factor (G-CSF or GCSF) is also known as colony-stimulating factor 3, CSF3, C17orf33, CSF3OS, GCSF, MGC45931. It is a glycoprotein, growth factor and cytokine produced by a number of different tissues to stimulate the bone marrow to produce granulocytes and stem cells. G-CSF then stimulates the bone marrow to release them into the blood. G-CSF also stimulates the survival, proliferation, differentiation, and function of neutrophil precursors and mature neutrophils. G-CSF regulates them using Janus kinase (JAK)/signal transducer and activator of transcription (STAT) and Ras /mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt) signal transduction pathway. G-CSF is produced by endothelium, macrophages, and a number of other immune cells. The natural human glycoprotein exists in two forms, a 174- and 180-amino-acid-long protein of molecular weight 19,600 grams per mole. G-CSF can effect on the hematopoietic system and neuronal cells as a neurotrophic factor. The action of G-CSF in the central nervous system is to induce neurogenesis, to increase the neuroplasticity and to counteract apoptosis. G-CSF stimulates the production of white blood cells (WBC). In oncology and hematology, a recombinant form of G-CSF is used with certain cancer patients to accelerate recovery from neutropenia after chemotherapy, allowing higher-intensity treatment regimens. Another form of recombinant human G-CSF called lenograstim is synthesised in Chinese Hamster Ovary cells (CHO cells). The recombinant human G-CSF synthesised in an E. coli expression system is called filgrastim.
  • 1: Schneider A,, et al., 2005, J. Clin. Invest. 115 (8): 2083–98.
  • 2: Pitzer C, et al., 2008, Brain 131 (Pt 12): 3335–47.

Disclaimer

  • FOR RESEARCH USE ONLY
    For additional information, visit ProSci's Terms & Conditions Page.
  • Disclaimer: Products are intended for laboratory research purposes only and should be used by qualified personnel only. They are not intended for use in humans. ProSci is not liable for damages or injuries resulting from receipt and/or use of ProSci materials. Please refer to the Material Safety Data Sheet (MSDS) for safe storage, handling, and use procedures.

CATALOG NUMBER: 96-785

  • Size: 0.05 mg
  • List Price: $660.00
Datasheet
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