I8659
Anti-Interferon-γ antibody produced in goat
affinity isolated antibody, lyophilized powder
Sinónimos:
Anti-IFN-γ
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About This Item
Productos recomendados
biological source
goat
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
human
technique(s)
immunohistochemistry: 5-15 μg/mL
neutralization: suitable
western blot: 0.1-0.2 μg/mL
UniProt accession no.
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... IFNG(3458)
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General description
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.
Anti-Interferon-γ recognizes human Interferon-γ.
Immunogen
purified, E. coli-derived recombinant human interferon γ.
Application
Anti-interferon-γ antibody may be used for immunoblotting at a working concentration of 0.1-0.2 μg/ml. For immunohistochemistry the recommended concentration is 5-15 μg/ml. The antibody has been used for immunohistochemistry of human cervical spinal cord sections using a concentration of 15 μg/ml. The antibody is suitable for neutralization reactions.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline 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
13 - Non Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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J Aebischer et al.
European journal of neurology, 19(5), 752-759 (2012-01-10)
Amyotrophic lateral sclerosis (ALS) is a paralytic and fatal neurodegenerative disorder caused by the gradual loss of both upper and lower motoneurons. There is compelling evidence from ALS experimental models that neuroinflammation actively contributes to motoneuron damage. We recently proposed
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
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
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
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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