I17001
Interferon-γ human
IFN-gamma, recombinant, expressed in HEK 293 cells, suitable for cell culture, endotoxin tested
Synonyme(s) :
IFN-γ
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About This Item
Produits recommandés
Produit recombinant
expressed in HEK 293 cells
Niveau de qualité
Pureté
≥98% (SDS-PAGE)
Forme
lyophilized powder
Puissance
≤0.250 ng/mL In Viral Resistance Assay ED50
Poids mol.
16 kDa (glycosylated)
Technique(s)
cell culture | mammalian: suitable
Adéquation
endotoxin tested
Température de stockage
−20°C
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Description générale
Interferon-γ (IFN-γ) is a pleotropic cytokine, encoded by the gene mapped to human chromosome 12q15. It is a non-covalent homodimer with two identical 17kDa polypeptide chains. It belongs to the type II class of interferons.
Recombinant human Interferon-γ (IFN-γ) is expressed in human 293 cells as a glycoprotein with a calculated molecular mass of 16 kDa. This protein is manufactured in human cells using an all-human production system, with full chemically defined ingredients and with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports better stability of the protein in culture. The bioactivity of IFN-γ expressed in human 293 cells is significantly higher compared to bacterially expressed IFN-γ.
Application
Interferon-γ human has been used in cytometric bead array to measure the levels of interferon-γ in the sample.
It has also been used for cytokine treatment of human islets to evaluate the activation of hypoxia inducible factor 1 α (HIF1α) targets, in vitro.
Actions biochimiques/physiologiques
IFN-γ is a dimerized soluble cytokine that is the only member of the type II class of interferons.
Interferon-γ (IFN-γ) plays an essential role in function of virtually all immune cells and both innate and adaptive immune responses. IFN-γ exhibits various biological effects, such as antiviral activity, inhibition of cell or tumor growth and promotion of terminal differentiation of B cells into immunoglobulin-producing cells. This cytokine also activates macrophages, increases cytotoxicity of natural killer cells and promotes T cell cytotoxicity. In addition to antiviral activity, recombinant human IFN-γ is a potent modulator of immune responses and modifies cellular processes.
Interferon-γ (IFN-γ) plays an essential role in function of virtually all immune cells and both innate and adaptive immune responses. IFN-γ exhibits various biological effects, such as antiviral activity, inhibition of cell or tumor growth and promotion of terminal differentiation of B cells into immunoglobulin-producing cells. This cytokine also activates macrophages, increases cytotoxicity of natural killer cells and promotes T cell cytotoxicity. In addition to antiviral activity, recombinant human IFN-γ is a potent modulator of immune responses and modifies cellular processes.
Séquence
QDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRG
Forme physique
Supplied as a lyophilized powder containing phosphate buffered saline.
Remarque sur l'analyse
The biological activity of recombinant human IFN-γ was tested in culture in a viral resistance assay. The ED50 is defined as the effective concentration of IFN-γ that allows 50% cell growth in an antiviral cell based bioassay.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
Expression and reconstitution of a biologically active mouse interferon gamma receptor in hamster cells. Chromosomal location of an accessory factor.
Hibino Y, et al.
The Journal of Biological Chemistry, 266(11), 6948-6951 (1991)
Class II cytokine receptors and their ligands: key antiviral and inflammatory modulators.
Renauld J C.
Nature Reviews: Immunology, 3(8), 667-667 (2003)
The IFNγ receptor: a paradigm for cytokine receptor signaling.
Bach E A, et al.
Annual Review of Immunology, 15(1), 563-591 (1997)
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Clinical use of interferon?γ.
Miller C H, et al.
Annals of the New York Academy of Sciences, 1182(1), 69-79 (2009)
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