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F9291

Sigma-Aldrich

Monoclonal ANTI-FLAG® BioM2 antibody produced in mouse

clone M2, purified immunoglobulin, buffered aqueous glycerol solution

Synonym(s):

Monoclonal ANTI-FLAG® M2 antibody produced in mouse, Anti-ddddk, Anti-dykddddk

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.32

biological source

mouse

Quality Level

200

conjugate

biotin conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M2, monoclonal

form

buffered aqueous glycerol solution

species reactivity

all

concentration

~1 mg/mL

technique(s)

dot blot: suitable (chemiluminescent detection)

isotype

IgG1

immunogen sequence

DYKDDDDK

shipped in

dry ice

storage temp.

−20°C

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General description

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.

Application

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.

Physical form

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

Preparation Note

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

Legal Information

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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Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

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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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Articles

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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