I9141
Anti-Interferon-γ antibody produced in goat
affinity isolated antibody, lyophilized powder
Synonym(s):
Anti-IFN-γ
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About This Item
MDL number:
UNSPSC Code:
51111800
biological source
goat
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
mouse
technique(s)
neutralization: suitable
western blot: suitable
UniProt accession no.
storage temp.
−20°C
Gene Information
mouse ... Ifng(15978)
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General description
Interferons (IFNs) are cytokines that are secreted in response to viral or bacterial infections and tumorigenesis. There are two types of IFNs, type I (IFN-α and IFN-β) and type II (IFN-γ). IFN-γ binds to specific receptor complex consisting of IFNγR1 and IFNγR2. There are many pathways that are mediated by IFN-γ binding such as JAK/STAT1, AP-1, NF-κB, STAT3 and STAT5. IFN-γ is pleotropic and performs various functions related to immune response, inflammation, differentiation and activation of T cells, cell cycle and apoptosis. The most studied function of IFN-γ is priming the antigen presenting cells by upregulating major histocompatibility (MHC) Class I molecules. IFN-γ has clinical applications in autoimmune diseases (rheumatoid arthritis), multiple sclerosis, cancer, HIV and fungal infections. Anti-Interferon-γ recognizes mouse Interferon-γ. It shows less than 1% cross reactivity with human IFN-γ.
Specificity
The antibody shows <1% cross-reactivity with recombinant human IFN-γ.
Immunogen
recombinant mouse IFN-γ.
Application
Anti-interferon-γ antibody may be used for immunoblotting at a working concentration of 0.1-0.2 μg/ml. The antibody is suitable for neutralization reactions.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline (pH 7.4) with 5% trehalose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Takuya Sekine et al.
Cell, 183(1), 158-168 (2020-09-28)
SARS-CoV-2-specific memory T cells will likely prove critical for long-term immune protection against COVID-19. Here, we systematically mapped the functional and phenotypic landscape of SARS-CoV-2-specific T cell responses in unexposed individuals, exposed family members, and individuals with acute or convalescent COVID-19. Acute-phase
Adithya Cattamanchi et al.
Journal of acquired immune deficiency syndromes (1999), 56(3), 230-238 (2011-01-18)
To determine whether interferon-gamma release assays (IGRAs) improve the identification of HIV-infected individuals who could benefit from latent tuberculosis infection therapy. Systematic review and meta-analysis. We searched multiple databases through May 2010 for studies evaluating the performance of the newest
Natalia Lubina-Dąbrowska et al.
Archivum immunologiae et therapiae experimentalis, 65(4), 325-338 (2017-03-17)
The aim of this study was to investigate the effects of interferon (IFN)-β1a and IFN-β1b treatment on inflammatory factors and myelin protein levels in the brain cortex of the Lewis rat experimental autoimmune encephalomyelitis (EAE), animal model of multiple sclerosis.
Leonidas C Platanias
Nature reviews. Immunology, 5(5), 375-386 (2005-05-03)
Interferons are cytokines that have antiviral, antiproliferative and immunomodulatory effects. Because of these important properties, in the past two decades, major research efforts have been undertaken to understand the signalling mechanisms through which these cytokines induce their effects. Since the
S E Ealick et al.
Science (New York, N.Y.), 252(5006), 698-702 (1991-05-03)
The x-ray crystal structure of recombinant human interferon-gamma has been determined with the use of multiple-isomorphous-replacement techniques. Interferon-gamma, which is dimeric in solution, crystallizes with two dimers related by a noncrystallographic twofold axis in the asymmetric unit. The protein is
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