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Key Documents

MAB8256

Sigma-Aldrich

Anti-Influenza A Antibody, H1N1 Antigen, clone 9B3.2

ascites fluid, clone 9B3.2, Chemicon®

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

9B3.2, monoclonal

Espèces réactives

human

Fabricant/nom de marque

Chemicon®

Technique(s)

immunofluorescence: suitable

Isotype

IgG2a

Conditions d'expédition

wet ice

Spécificité

Influenza A H1N1 antigen.
• Reacts strongly with all H1N1 strains tested including Beijing, A/ Texas /36/91, A/Berkeley/1/98, A/HongKong/503/97, A/Nanchang /16A/98,A/PR/8/34, New Caledonia strain, and A/California/7/2009.
• No reactivity shown to Influenza B strains.

Immunogène

Epitope: H1N1 Antigen
Influenza blend

Application

Anti-Influenza A Antibody, H1N1 Antigen, clone 9B3.2 is an antibody against Influenza A for use in IF.
Indirect Immunofluorescence : 1/32
Research Category
Infectious Diseases
Research Sub Category
Infectious Diseases - Viral

Forme physique

Ascites

Stockage et stabilité

Maintain at -20°C. Avoid repeated freeze/thaw cycles.

Informations légales

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Sreekumar Othumpangat et al.
Pathogens (Basel, Switzerland), 12(1) (2023-01-22)
Understanding the host response to influenza A virus (IAV) infection is vital for developing intervention strategies. The primary barriers for invading respiratory pathogens are the respiratory tract epithelial cells and antimicrobial proteins generated by these cells. The antimicrobial peptide, β-defensin-1
Rapid typing, subtyping and RNA quantification of influenza virus type A strains in respiratory secretions.
Elena Percivalle,Francesca Rovida,Antonio Piralla,Vanina Rognoni,Maurizio Zavattoni et al.
The New Microbiologica null
Brian J Morrison et al.
Journal of virological methods, 248, 7-18 (2017-06-19)
This study describes an antibody-dependent NK cell degranulation assay, as a biomarker to assess antibody-dependent cellular cytotoxicity (ADCC) response in influenza plasma and for antibody therapies against influenza infection. The concentration of neutralizing antibodies (NAbs) against the hemagglutinin receptor of
Asami Makino et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 31(4), 1301-1322 (2016-08-06)
We identified a novel, nontoxic mushroom protein that specifically binds to a complex of sphingomyelin (SM), a major sphingolipid in mammalian cells, and cholesterol (Chol). The purified protein, termed nakanori, labeled cell surface domains in an SM- and Chol-dependent manner
Pilgyu Kang et al.
Scientific reports, 5, 12087-12087 (2015-07-15)
Biomolecular interactions, such as antibody-antigen binding, are fundamental to many biological processes. At present, most techniques for analyzing these interactions require immobilizing one or both of the interacting molecules on an assay plate or a sensor surface. This is convenient

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