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Safety Information

I5027

Sigma-Aldrich

Anti-Interferon-γ antibody produced in goat

affinity isolated antibody, lyophilized powder

Synonym(s):

Anti-IFN-γ

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About This Item

MDL number:
MFCD00162308
UNSPSC Code:
51111800
NACRES:
NA.41

biological source

goat

Quality Level

100

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

mouse, rat

technique(s)

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

UniProt accession no.

P01581

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

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Immunogen

recombinant rat interferon-γ expressed in E. coli.

Biochem/physiol Actions

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.

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 Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

I5027-VAR:
I5027-.1MG:
I5027-BULK:
I5027-.1MG-PW:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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