The purity of recombinant hIFN-γ was determined by SDS-PAGE of 1.5 µg reduced (+) and non-reduced (-) recombinant hIFN-γ and staining overnight with Coomassie Blue.Learn more about how we get our images
The bioactivity of recombinant hIFN-γ was determined in a virus protection assay. A549 cells were pretreated with increasing concentrations of hIFN-γ (started at 2.5 ng/ml). Cells were then innoculated with encephalomyocarditis virus (EMCV). The OD595 was determined for the surviving cells.Learn more about how we get our images
Western blot analysis of extracts from HeLa cells, untreated or treated with hIFN-γ for 20 minutes, using Phospho-Stat3 (Tyr705) (D3A7) XP® Rabbit mAb #9145 (upper) and Stat3 (124H6) Mouse mAb #9139 (lower).Learn more about how we get our images
Recombinant human IFN-γ was expressed in E. coli and is supplied in a lyophilized form. A greater than 95% purity was determined by SDS-PAGE. Endotoxin levels are less than or equal to 1 EU / 1 μg hIFN-γ.
The bioactivity of hIFN-γ was determined in a virus protection assay. The ED50 of each lot is between 0.30-1.2 ng/ml.
Working concentration of hIFN-γ generally ranges from 0.1-10 ng/ml.
Recombinant human IFN-γ is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long term storage.
IFN-γ plays key roles in both the innate and adaptive immune response. IFN-γ activates the cytotoxic activity of innate immune cells such as macrophages and NK cells (1,2). IFN-γ production by NK cells and antigen-presenting cells (APCs) promotes the cell-mediated adaptive immunity by inducing IFN-γ production by T lymphocytes, increasing expression of class I and class II MHC, and enhancing peptide antigen presentation (1). The anti-viral activity of IFN-γ is due to its induction of PKR and other regulatory proteins. Binding of IFN-γ to the IFNGR1/IFNGR2 complex promotes dimerization of the receptor complexes. Binding induces a conformational change in receptor intracellular domains and signaling involves Jak1, Jak2 and Stat1 (3). The critical role of IFN-γ in amplification of immune surveillance and function is supported by increased susceptibility to pathogen infection in IFN-γ or IFNGR knockout mice and in humans with inactivating mutations in IFNGR1 or IFNGR2. IFN-γ also appears to have a role in atherosclerosis (4).
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