Name:
IFN-γ Protein
Synonyms:
IFN-γ, Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma
Species Name:
Canine
Label Name:
No Tag
Marker Name:
Unconjugated
Accession:
P42161
Gene Id:
Gln24-Lys166 QAMFFKEIENLKEYFNASNPDVSDGGSLFVDILKKWREESDKTIIQSQIVSFYLKLFDNFKDNQIIQRSMDTIKEDMLGKFLNSSTSKREDFLKLIQIPVNDLQVQRKAINELIKVMNDLSPRSNLRKRKRSQNLFRGRRASK
Molecular Weight:
16kDa (Reducing)
Purity:
>95% by SDS-PAGE
Physical Appearance Name:
Lyophilized Powder
Endotoxin Name:
<0.1EU/μg
Reconstitution:
Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
Stability Storage:
·12 months from date of receipt, -20 to -70 °C as supplied. ·1 month, 2 to 8 °C under sterile conditions after reconstitution. ·Please avoid repeated freeze-thaw cycles.
Buffer System:
20mM Tris, 300mM NaCl, pH8.0
Quality Statement:
Interferon gamma (IFN-γ) is a cytokine critical to both innate and adaptive immunity, and functions as the primary activator of macrophages, in addition to stimulating natural killer cells and neutrophils. A non-IgE-mediated anaphylactic reaction and severe bronchospasm have been reported once after the first injection of interferon gamma. IFN-γ activates cells via a different receptor than IFN-α and IFN-β, which accounts for the different physiological properties of the proteins. Production of IFN-γ is largely restricted to activated CD4+ TH1 T cells, CD8+ T cells, and natural killer cells. One of the most important consequences of IFN-γ secretion is the activation of macrophages. In addition, IFN-γ plays a central role in inflammatory responses by activating endothelial cells, promoting TH1 cell development and cellular immune responses, and up-regulation of major histocompatability complex protein expression on antigen-presenting cells.
Reference:
1.Goshima N. et al. (2008) Human protein factory for converting the transcriptome into an in vitro-expressed proteome. Nomura N Nat Methods. 5: 1011-7. 2.Thiel D J. et al. (2000) Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex. Structure. 8(9): 927-936. 3.Schoenborn J R. et al. (2007) Regulation of interferon-gamma during innate and adaptive immune responses. Adv Immunol. 96: 41-101.
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