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I8659

Sigma-Aldrich

Anti-Interferon-γ antibody produced in goat

affinity isolated antibody, lyophilized powder

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Synonym(s):
Anti-IFN-γ
MDL number:
NACRES:
NA.41

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.

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.

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)


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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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