Detects human IFN-gamma in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 50% cross-reactivity with recombinant rhesus monkey IFN‑ gamma is observed, and less than 5% cross-reactivity with recombinant mouse IFN‑ gamma, recombinant canine IFN‑ gamma, recombinant porcine IFN‑ gamma, recombinant bovine IFN‑ gamma, recombinant rat IFN‑ gamma, recombinant feline IFN‑ gamma, and recombinant equine IFN‑ gamma is observed.
Polyclonal Goat IgG
Protein A or G purified
E. coli-derived recombinant human IFN-gamma Met1-Gln144 Accession # Q14609
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize IFN‑ gamma inhibition of EMCV-induced cytopathy in the HeLa human cervical epithelial carcinoma cell line [Meager, A. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 129]. The Neutralization Dose (ND50) is typically 1-5 µg/mL in the presence of 5 ng/mL Recombinant Human IFN‑ gamma.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
IFN‑ gamma Inhibition of EMCV-induced Cytopathy and Neutralization by Human IFN‑ gamma Antibody. Recombinant Human IFN‑ gamma (Catalog # 285-IF) reduces the Encephalomyocarditis Virus (EMCV)-induced cytopathy in the HeLa human cervical epithelial carcinoma cell line in a dose-dependent manner (orange line), as measured by crystal violet staining. Inhibition of EMCV activity elicited by Recombinant Human IFN‑ gamma (5 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human IFN‑ gamma Polyclonal Antibody (Catalog # AB‑285‑NA). The ND50 is typically 1‑5 µg/mL.
Preparation and Storage
Reconstitute at 1 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Interferon-gamma (IFN-gamma ), also known as type II or immune interferon, exerts a wide range of immunoregulatory activities and is considered to be the prototype proinflammatory cytokine (1, 2). Mature human IFN-gamma exists as a non-covalently linked homodimer of 20-25 kDa variably glycosylated subunits (3). It shares 90% amino acid (aa) sequence identity with rhesus IFN-gamma, 59-64% with bovine, canine, equine, feline, and porcine IFN‑ gamma, and 37-43% with cotton rat, mouse, and rat IFN-gamma. IFN-gamma dimers bind to IFN-gamma RI (alpha subunits) which then interact with IFN-gamma RII (beta subunits) to form the functional receptor complex of two alpha and two beta subunits. Inclusion of IFN-gamma RII increases the binding affinity for ligand and the efficiency of signal transduction (4, 5). IFN-gamma is produced by a variety of immune cells under inflammatory conditions, notably by T cells and NK cells (6). It plays a key role in host defense by promoting the development and activation of Th1 cells, chemoattraction and activation of monocytes and macrophages, upregulation of antigen presentation molecules, and immunoglobulin class switching in B cells. It also exhibits anti-viral, anti-proliferative, and apoptotic effects (6, 7). In addition, IFN-gamma functions as an anti-inflammatory mediator by promoting the development of regulatory T cells and inhibiting Th17 cell differentiation (8, 9). The pleiotropic effects of IFN-gamma contribute to the development of multiple aspects of atherosclerosis (7).
Billiau, A. and P. Matthys (2009) Cytokine Growth Factor Rev. 20:97.
Pestka, S. et al. (2004) Immunol. Rev. 202:8.
Gray, P.W. and D.V. Goeddel (1982) Nature 298:859.
Marsters, S.A. et al. (1995) Proc. Natl. Acad. Sci. USA 92:5401.
Krause, C.D. et al. (2000) J. Biol. Chem. 275:22995.
Schroder, K. et al. (2004) J. Leukoc. Biol. 75:163.
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