I8659
Anti-Interferon-γ antibody produced in goat
affinity isolated antibody, lyophilized powder
Sinônimo(s):
Anti-IFN-γ
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About This Item
Produtos recomendados
fonte biológica
goat
Nível de qualidade
conjugado
unconjugated
forma do anticorpo
affinity isolated antibody
tipo de produto de anticorpo
primary antibodies
clone
polyclonal
forma
lyophilized powder
reatividade de espécies
human
técnica(s)
immunohistochemistry: 5-15 μg/mL
neutralization: suitable
western blot: 0.1-0.2 μg/mL
nº de adesão UniProt
temperatura de armazenamento
−20°C
modificação pós-traducional do alvo
unmodified
Informações sobre genes
human ... IFNG(3458)
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Descrição geral
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.
Imunogênio
purified, E. coli-derived recombinant human interferon γ.
Aplicação
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.
forma física
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline with 5% trehalose.
Exoneração de responsabilidade
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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recomendado
Código de classe de armazenamento
13 - Non Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
Certificados de análise (COA)
Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “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
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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