I9016
Anti-Interferon-γ antibody produced in goat
IgG fraction of antiserum
Synonym(s):
Anti-IFN-γ
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About This Item
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biological source
goat
Quality Level
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human
technique(s)
neutralization: suitable
western blot: suitable
UniProt accession no.
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... IFNG(3458)
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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 human Interferon-γ. It does not bind specifically to mouse, hamster or bovine IFN-γ.
Anti-Interferon-γ recognizes human Interferon-γ. It does not bind specifically to mouse, hamster or bovine IFN-γ.
Specificity
The antibody shows no cross-reactivity with recombinant mouse IFN-γ.
Immunogen
recombinant human IFN-γ.
Application
Anti-interferon-γ antibody may be used for immunoblotting at a working concentration of 1-2 μg/ml. The antibody is suitable for neutralization reactions.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing carbohydrates.
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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recommended
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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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
M Raza Zaidi et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 17(19), 6118-6124 (2011-06-28)
Interferon-γ is a cytokine whose biological activity is conventionally associated with cytostatic/cytotoxic and antitumor mechanisms during cell-mediated adaptive immune response. It has been used clinically to treat a variety of malignancies, albeit with mixed results and side effects that can
Kate Schroder et al.
Journal of leukocyte biology, 75(2), 163-189 (2003-10-04)
Interferon-gamma (IFN-gamma) coordinates a diverse array of cellular programs through transcriptional regulation of immunologically relevant genes. This article reviews the current understanding of IFN-gamma ligand, receptor, signal transduction, and cellular effects with a focus on macrophage responses and to a
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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