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Documenti fondamentali

F9291

Sigma-Aldrich

Anticorpo monoclonale ANTI-FLAG® M2

clone M2, purified immunoglobulin, buffered aqueous glycerol solution

Sinonimo/i:

Anti-ddddk, Anti-dykddddk

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.32

Origine biologica

mouse

Coniugato

biotin conjugate

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

M2, monoclonal

Stato

buffered aqueous glycerol solution

Reattività contro le specie

all

Concentrazione

~1 mg/mL

tecniche

dot blot: suitable (chemiluminescent detection)

Isotipo

IgG1

Sequenza immunogenica

DYKDDDDK

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

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Descrizione generale

The monoclonal Anti-FLAG BioM2 mouse antibody is covalently attached to biotin by hydrazide linkage. The antibody recognizes the FLAG sequence at the N-terminus, Met-N-terminus or C-terminus of FLAG fusion porteins.

Applicazioni

Biotin-labeled antibody is used for immunodetection methods using avidin- or streptavidin-conjugated reporter enzymes such as streptavidin-peroxidase. Primary antibody conjugates are preferred when using murine cells as the recombinant protein host.
Antibody is suitable for immunofluorescence, western blotting, microscopy applications and for the formation of avidin-biotin complexes.

Learn more product details in our FLAG® application portal.

Stato fisico

Solution in 50% glycerol, 10 mM sodium phosphate, pH 7.25, containing 150 mM NaCl and 0.02% sodium azide

Nota sulla preparazione

Dilute antibody in TBS (.05M Tris, pH7.4, with .15M NaCl) to a final concentration of 1-10μg/mL.

Note legali

ANTI-FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

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Certificati d'analisi (COA)

Lot/Batch Number
SLCJ4779
SLCF0628
SLBX7801
SLBW9130
SLBV8846

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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

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Hong-Won Lee et al.
Nature communications, 4, 1505-1505 (2013-02-21)
Co-immunoprecipitation (co-IP) has become a standard technique, but its protein-band output provides only static, qualitative information about protein-protein interactions. Here we demonstrate a real-time single-molecule co-IP technique that generates real-time videos of individual protein-protein interactions as they occur in unpurified
Yoori Kim et al.
Scientific reports, 7(1), 2071-2071 (2017-05-20)
Single-molecule studies of protein-nucleic acid interactions frequently require site-specific modification of long DNA substrates. The bacteriophage λ is a convenient source of high quality long (48.5 kb) DNA. However, introducing specific sequences, tertiary structures, and chemical modifications into λ-DNA remains technically
Helen Hwang et al.
Scientific reports, 4, 6391-6391 (2014-09-30)
The ends of eukaryotic chromosomes are capped by telomeres which consist of tandem G-rich DNA repeats stabilized by the shelterin protein complex. Telomeres shorten progressively in most normal cells due to the end replication problem. In more than 85% of
Qing Xu et al.
Nature communications, 8(1), 425-425 (2017-09-06)
Tumor necrosis factor (TNF) has a critical role in diverse cellular events including inflammation, apoptosis and necroptosis through different signaling complexes. However, little is known about how the transition from inflammatory signaling to the engagement of death pathways is modulated.
Kenichiro Kawai et al.
PloS one, 6(11), e27106-e27106 (2011-11-11)
Nanoparticles (NPs) are small entities that consist of a hydroxyapatite core, which can bind ions, proteins, and other organic molecules from the surrounding environment. These small conglomerations can influence environmental calcium levels and have the potential to modulate calcium homeostasis
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Articoli

Glycan Labeling

Structural modifications of proteins are essential to living cells. When aberrantly regulated they are often the basis of disease. Glycans are responsible for much of the structural variation in biologic systems, and their representation on cell surfaces is commonly called the “glycome.”

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