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I5027

Sigma-Aldrich

Anti-Interferon-γ antibody produced in goat

affinity isolated antibody, lyophilized powder

Synonyme(s) :

Anti-IFN-γ

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About This Item

Numéro MDL:
MFCD00162308
Code UNSPSC :
51111800
Nomenclature NACRES :
NA.41

Source biologique

goat

Niveau de qualité

100

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

lyophilized powder

Espèces réactives

mouse, rat

Technique(s)

immunohistochemistry: 5-15 μg/mL
neutralization: suitable
western blot: 0.1-0.2 μg/mL

Numéro d'accès UniProt

P01581

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

mouse ... Ifng(15978)
rat ... Ifng(25712)

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Immunogène

recombinant rat interferon-γ expressed in E. coli.

Actions biochimiques/physiologiques

Interferons (IFNs) are cytokines that are secreted in response to viral or bacterial infections and tumorigenesis. 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.

Forme physique

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline with 5% trehalose.

Clause de non-responsabilité

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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Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
J Aebischer et al.
Cell death and differentiation, 18(5), 754-768 (2010-11-13)
Amyotrophic lateral sclerosis (ALS) is an incurable neurodegenerative disease that primarily affects motoneurons in the brain and spinal cord. Dominant mutations in superoxide dismutase-1 (SOD1) cause a familial form of ALS. Mutant SOD1-damaged glial cells contribute to ALS pathogenesis by
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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