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Recombinant Human IFN-γ

Recombinant Human IFN-γ

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Recombinant Human Interferon-Gamma (IFN-γ)Purified No Carrier Protein(Immune Interferon, Type II Interferon, T Cell Interferon, MAF, IFNG, IFG, IFI)Prod. No.: I-179 Source E. coli Pkg. Size: 1 mg, 100 μg Storage: 2°C to 8°C

Recombinant Human Interferon-Gamma (IFN-γ)
Purified No Carrier Protein
(Immune Interferon, Type II Interferon, T Cell Interferon, MAF, IFNG, IFG, IFI)
Prod. No.: I-179
Source E. coli
Pkg. Size: 1 mg, 100 µg
Storage: 2°C to 8°C

Description
Background:

Interferon-gamma (IFN-γ) or type II interferon is a dimerized soluble cytokine that is the only member of the type II class of interferons.1 It is a cytokine critical for innate and adaptive immunity against viral and intracellular bacterial infections and for tumor control. IFNG is produced predominantly by natural killer (NK) and natural killer T (NKT) cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte (CTL) effector T cells once antigen-specific immunity develops.2 IFN-γ has antiviral, immunoregulatory, and anti-tumour properties.3

Source
E. coli
Molecular Weight
The predicted molecular weight of Recombinant Human IFN-γ is Mr 16.9 kDa.
State of Matter
Solution
Formulation
This recombinant protein solution was 0.2 µm filtered and formulated in modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives present.
Purity
>97% by SDS-PAGE and analyzed by silver stain.
Storage and Stability
This recombinant protein solution can be stored at 2° - 8°C for six months without detectable loss of activity. Do not freeze.
Endotoxin
<1.0 EU/µg as determined by the LAL method
Biological Activity
The biological activity of Human IFN-Gamma was measured in anti-viral assays using HeLa cells infected with EMC virus (Meager, A., 1987, Lymphokines and Interferons, a Practical Approach, Clemens, M.J., Morris, A.G. and Gearing, A.J.H. eds., IRL Press, p. 129). The expected ED50 for this effect is typically 0.3 - 1.5 ng/ml.
Each investigator should determine their own optimal working dilution for specific applications.
Amino Acid Sequence

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References
1. Goeddel DV et al. (1982) Nature 298: 859
2. Wilson CB et al. (2007) Adv. Immunol. 96: 41
3. Hume DA et al. (2004) J Leukoc Biol. 75: 163
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