G0407

Granulocyte colony-stimulating factor human

>97% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture

• UNSPSC Code: 12352202
• NACRES: NA.77
• MDL number: MFCD00166475
• Biological source: human
• Recombinant: expressed in E. coli
• Assay: >97% (SDS-PAGE)
• Form: lyophilized powder
• Mol wt: 18.8 kDa (175 amino acids including N-terminal methionine)
• Impurities: <0.10 EU/μg

Propiedades

• Nombre del producto: Granulocyte colony-stimulating factor human, >97% (SDS-PAGE), G-CSF, recombinant, expressed in E. coli, suitable for cell culture
• biological source: human
• Quality Segment: 100
• recombinant: expressed in E. coli
• assay: >97% (SDS-PAGE)
• form: lyophilized powder
• potency: 0.01-0.1 ng/mL
• quality: endotoxin tested
• mol wt: 18.8 kDa (175 amino acids including N-terminal methionine)
• packaging: pkg of 5 and 25 μg
• technique(s): cell culture | mammalian: suitable
• impurities: <0.10 EU/μg
• UniProt accession no.: P09919
• storage temp.: −20°C

Descripción

General description

Granulocyte colony-stimulating factor human (GCSF) gene is mapped to human chromosome 17q21.1.[1] Structurally, GCSF comprises a four α-helical bundle.[2]

Application

Granulocyte colony-stimulating factor human has been used:

• in culturing human neutrophils[3]
• as a growth factor component of double layer granulocyte-macrophage colony-forming unit (CFU-GM) culture system for CD34⁺ cells
• to test its protective effects chronic liver damage model[4]

Biochem/physiol Actions

Granulocyte colony-stimulating factor human (GCSF) interacts specifically with the immunoglobin (Ig) domain of the granulocyte colony-stimulating factor receptor (GCSFR).[2]

Granulocyte-colony stimulating factor (G-CSF) is a proliferation, differentiation, survival, and activation factor for hematopoietic cells of the restricted neutrophilic granulocyte lineage. It is produced by macrophages activated by endotoxin (LPS), by monocytes activated by TNF-α with IFNγ, by fibroblasts and endothelial cells activated by IL-1 or TNF-α, and by bone marrow stromal cells activated by IL-1 or LPS. It is suggested that during the inflammatory process endotoxins stimulate tissue macrophages to produce not only G-CSF but several other cytokines, including IL-1 and TNF-α, which in turn stimulate more G-CSF release from endothelial cells and fibroblasts. G-CSF can also synergize with IL-3 to shorten the G₀ period of early hematopoietic progenitors. In addition to the namesake proliferative activity, G-CSF acts on mature neutrophils to enhance their survival and to stimulate their tumorcidal activity. Human G-CSF binds and activates a 130 kD to150 kD glycoprotein single chain receptor that has been classified as a member of the hematopoietic (cytokine) receptor family, the cytokine receptor class I, or the gp130 related cytokine receptor family (although it does not apparently bind to gp130). G-CSF receptors can be found on neutrophils, myeloid leukemia cells that respond to G-CSF, bone marrow cells of neutrophilic granulocyte lineage, and on placental trophoblasts, plus a soluble form may be expressed. Two forms of human G-CSF (177 and 174 amino acids) are synthesized from a single gene by alternative splicing, but murine G-CSF is a single expressed form of 178 amino acids. Human and murine G-CSF share 73% amino acid sequence homology and full cross-reactivity.

Physical form

Lyophilized from 0.2 μm-filtered solution of 10 mM HOAc, pH 3.5, containing 50 μg BSA per μg G-CSF

Analysis Note

The biological activity is measured in a cell proliferation assay using a murine myeloblastic cell line, NFS-60.

Información de seguridad

• Clase de almacenamiento: 11 - Combustible Solids
• wgk: WGK 3
• ppe: Eyeshields, Gloves, type N95 (US)
• flash_point_f: No data available
• flash_point_c: No data available