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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

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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Yingru Liu et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 30(6), 2025-2038 (2010-02-12)
To assess the effects and mechanisms of a CD200R1 agonist administered during the progressive stage of a multiple sclerosis model, we administered CD200R1 agonist (CD200Fc) or control IgG2a during the chronic phase of disease (days 10-30) in mice with experimental
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
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
Nawal Bendris et al.
PloS one, 6(7), e22879-e22879 (2011-08-11)
Cyclin A2 is essential at two critical points in the somatic cell cycle: during S phase, when it activates CDK2, and during the G2 to M transition when it activates CDK1. Based on the crystal structure of Cyclin A2 in
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

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