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Merck
CN

MAB8256

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

ascites fluid, clone 9B3.2, Chemicon®

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Clone:
9B3.2, monoclonal
Species reactivity:
human
Application:
immunofluorescence
Technique(s):
immunofluorescence: suitable
Citations:
6
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产品名称

Anti-Influenza A Antibody, H1N1 Antigen, clone 9B3.2, ascites fluid, clone 9B3.2, Chemicon®

biological source

mouse

antibody form

ascites fluid

antibody product type

primary antibodies

clone

9B3.2, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

immunofluorescence: suitable

isotype

IgG2a

shipped in

wet ice

Quality Level

Application

Research Sub Category
Infectious Diseases - Viral
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

Biochem/physiol Actions

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.

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.

Immunogen

Epitope: H1N1 Antigen
Influenza blend

Physical form

Ascites

Preparation Note

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

Legal Information

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

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存储类别

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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
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
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
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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