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Monoclonal ANTI-FLAG® M1 antibody produced in mouse

clone M1, purified immunoglobulin, buffered aqueous solution

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Anti-ddddk, Anti-dykddddk
MDL number:

biological source


Quality Level



antibody form

purified immunoglobulin

antibody product type

primary antibodies


M1, monoclonal


buffered aqueous solution

purified by

using Protein A

species reactivity



2-5 mg/mL


western blot: 10 μg/mL

immunogen sequence


shipped in

dry ice

storage temp.


Related Categories

General description

The ANTI-FLAG M1 IgG2b mooclonal antibody binds to proteins with a FLAG marker at the free N-terminus.

Method of purification - Protein A


FLAG; peptide sequence DYKDDDDK


Monoclonal ANTI-FLAG® M1 antibody produced in mouse is suitable for immunoprecipitation, western blotting, or EIA in yeast, animal and E.coli cells.

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Chromatin immunoprecipitation (1 paper)
Immunofluorescence (1 paper)

Learn more product details in our FLAG® applications portal.

Biochem/physiol Actions

Binds to the FLAG epitope when it is located at the free amino-terminus of a fusion protein. Does not bind to Met-FLAG fusion proteins, so will not recognize unprocessed, cytoplasmically expressed proteins. Binding is Ca2+-dependent; the complex dissociates in the absence of calcium ions.

Physical form

Solution in 10 mM sodium phosphate, 150 mM NaCl, pH 7.4, containing 0.02% sodium azide (w/v).

Preparation Note

Dilute antibody to 10ug/mL in .05 M TBS, pH 7.4, containing 1 mM CaCl2.

Legal Information

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

Storage Class

10 - Combustible liquids




Not applicable


Not applicable

Certificates of Analysis (COA)

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Min Luo et al.
Cell research, 20(2), 211-222 (2010-01-27)
As a critical apoptosis executioner, caspase-3 becomes activated and then enters into the nucleus to exert its function. However, the molecular mechanism of this nuclear entry of active caspase-3 is still unknown. In this study, we revealed that caspase-3 harbors
Mohammad Al Sorkhy et al.
BMC cancer, 12, 45-45 (2012-01-28)
Spy1 is a novel 'cyclin-like' activator of the G1/S transition capable of enhancing cell proliferation as well as inhibiting apoptosis. Spy1 protein levels are tightly regulated during normal mammary development and forced overexpression in mammary mouse models accelerates mammary tumorigenesis.
Reem Berro et al.
Journal of virology, 82(14), 7155-7166 (2008-05-16)
The human immunodeficiency virus type 1 (HIV-1) Tat is a 14-kDa viral protein that acts as a potent transactivator by binding to the transactivation-responsive region, a structured RNA element located at the 5' end of all HIV-1 transcripts. Tat transactivates
Andrew Best et al.
Nature communications, 5, 4760-4760 (2014-09-12)
Alternative splicing--the production of multiple messenger RNA isoforms from a single gene--is regulated in part by RNA binding proteins. While the RBPs transformer2 alpha (Tra2α) and Tra2β have both been implicated in the regulation of alternative splicing, their relative contributions
Jaana M Jurvansuu et al.
PloS one, 6(9), e25317-e25317 (2011-10-08)
Transmembrane protein 18 (TMEM18) has previously been connected to cell migration and obesity. However, the molecular function of the protein has not yet been described. Here we show that TMEM18 localises to the nuclear membrane and binds to DNA in

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