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Key Documents

G0282

Sigma-Aldrich

Granulocyte-Macrophage Colony-Stimulating Factor from mouse

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

Synonyme(s) :

GM-CSF

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

product name

Granulocyte-Macrophage Colony-Stimulating Factor from mouse, GM-CSF, from mouse, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture

Source biologique

mouse

Niveau de qualité

Produit recombinant

expressed in E. coli

Pureté

≥97% (SDS-PAGE)

Forme

lyophilized powder

Puissance

≤0.2 ng/mL EC50 (corresponds to ≥5 × 106 units/mg)

Qualité

endotoxin tested

Poids mol.

~15 kDa (125 amino acids including N-terminal methionine)

Conditionnement

pkg of 5 and 50 μg

Conditions de stockage

avoid repeated freeze/thaw cycles

Technique(s)

cell culture | mammalian: suitable

Impuretés

≤1 EU/mg

Couleur

white

Solubilité

water: soluble, clear, colorless

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

Actions biochimiques/physiologiques

Granulocyte-macrophage colony stimulating factor (GM-CSF) is a growth and differentiation factor for cells in the granulocyte, macrophage and eosinophil lineage. GM-CSF stimulates colony formation from pluripotential progenitor cells at extremely low concentrations and is an essential survival and proliferative factor for hematopoietic progenitor cells in all divisions up to maturity. It also stimulates growth in some epithelial cells and osteoclasts. GM-CSF is produced by a variety of cell types (monocytes, endothelial cells, T-cells, fibroblasts, mitogen-stimulated B-cells, and LPS-stimulated macrophages). GM-CSF is secreted as a single chain glycoprotein containing 128 amino acids for human with a conserved disulfide bond. Human and murine GM-CSF share approx. 54% sequence homology and do not cross-react in bioactivity.

Forme physique

Lyophilized from 10 mM acetic acid plus 250 μg BSA.

Remarque sur l'analyse

The EC50 activity of mouse GM-CSF is tested in culture using murine FDP-1 cells.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

M A Guthridge et al.
Stem cells (Dayton, Ohio), 16(5), 301-313 (1998-10-10)
The process of ligand binding leading to receptor activation is an ordered and sequential one. High-affinity binding of GM-CSF, interleukin 3 (IL-3), and IL-5 to their receptors induces a number of key events at the cell surface and within the
R C Skoda
Journal of receptor and signal transduction research, 19(1-4), 741-772 (1999-03-11)
The helical cytokines constitute a family of proteins with a common three-dimensional structure. They exert a wide variety of biological effects with a preference for the hematopoietic system. The effects of helical cytokines are mediated by cell surface receptors, which
A Kelso
Immunology and cell biology, 76(4), 300-317 (1998-09-02)
Cytokines participate in the induction and effector phases of all immune and inflammatory responses. They are therefore obvious tools and targets for strategies designed to promote, inhibit or redirect these responses. However, the complexity of the cytokine network has hindered
M H Heim
Journal of receptor and signal transduction research, 19(1-4), 75-120 (1999-03-11)
The Jak-STAT pathway was originally discovered through the study of interferon induced intracellular signal transduction. Meanwhile, a large number of cytokines, hormones and growth factors have been found to activate Jaks and STATs. Jaks (Janus Kinases) are a unique class
Bin Ji et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 28(47), 12255-12267 (2008-11-21)
We demonstrate the significance of peripheral benzodiazepine receptor (PBR) imaging in living mouse models of Alzheimer's disease (AD) as biomarkers and functional signatures of glial activation. By radiochemically and immunohistochemically analyzing murine models of the two pathological hallmarks of AD

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