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A8592

Sigma-Aldrich

Monoclonal ANTI-FLAG® M2-Peroxidase (HRP) 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:
41106514
NACRES:
NA.32

biological source

mouse

Quality Level

conjugate

peroxidase 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)

indirect ELISA: 1:20,000

isotype

IgG1

immunogen sequence

DYKDDDDK

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... GPX1(2876)

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General description

The Monoclonal ANTI-FLAG M2-Peroxidase is a mouse IgG antibody covalently conjugated to horseradish peroxidase ( HRP). The antibody binds to FLAG fusion proteins and recognizes the FLAG epitope at N-terminal, Met-N-terminal, C-terminal, and internal FLAG peptides.

Application

For simple, one-step detection by immunocytochemistry, ELISA, or Western blotting. Especially useful in detection of FLAG fusion proteins expressed in murine host, where secondary anti-mouse antibodies may cause cross-reactivity.
Suggested dilution for immunocytochemistry and western blotting 1:100 to 1:1000
Suggested dilution for ELISA 1:20,000

Learn more product details in our FLAG® application portal.

Physical form

Solution in phosphate buffered saline containing 50% glycerol plus preservative and stabilizer

Preparation Note

Dilute ANTI-FLAG M2-Peroxidase solution in Tris Buffered Saline (TBS): 0.05 M Tris, pH 7.4, with 0.15 M NaCl.

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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Danger

Hazard Classifications

Aquatic Acute 1 - Aquatic Chronic 1 - Eye Dam. 1 - Skin Corr. 1C - Skin Sens. 1

Storage Class

8A - Combustible corrosive hazardous materials

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Mickaël Lelek et al.
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The Journal of biological chemistry, 288(46), 33171-33180 (2013-10-08)
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The 200-kDa L protein of arenaviruses plays a central role in viral genome replication and transcription. This study aimed at providing evidence for the domain structure of L protein by combining bioinformatics with a stepwise mutagenesis approach using the Lassa

Articles

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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