MilliporeSigma
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F7425

Millipore

ANTI-FLAG® antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-ddddk, Anti-dykddddk
MDL number:
NACRES:
NA.32

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

all

concentration

~0.8 mg/mL

technique(s)

dot blot: 1-2.5 μg/mL
immunoprecipitation (IP): 4-8 μg using amino terminal FLAG-BAP fusion protein from E. coli crude lysate
indirect immunofluorescence: 5-10 μg/mL using 293T cells transfected with a plasmid encoding FLAG-JNK
western blot (chemiluminescent): 1-2.5 μg/mL using an E. coli periplasmic extract expressing an N-terminal FLAG fusion protein

isotype

IgG

immunogen sequence

DYKDDDDK

shipped in

dry ice

storage temp.

−20°C

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F2555F3040F4049
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

FITC conjugate

antibody form

affinity isolated antibody

antibody form

ascites fluid

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

clone

polyclonal

clone

SIG1-25, monoclonal

clone

M1, monoclonal

clone

M2, monoclonal

form

buffered aqueous solution

form

-

form

buffered aqueous solution

form

buffered aqueous solution

species reactivity

all

species reactivity

-

species reactivity

all

species reactivity

all

General description

The FLAG epitope, is an eight amino acid protein with an enterokinase-cleavage site.
The rabbit Anti-FLAG polyclonal affinity antibody ANTI-FLAG recognizes the FLAG epitope located on FLAG fusion proteins. This antibody reacts with N-terminal, N-terminal-Met, and C-terminal FLAG fusion proteins.

Immunogen

FLAG; peptide sequence DYKDDDDK

Application

The antibody recognizes the FLAG epitope located on FLAG-tagged fusion proteins at the N-terminus or C-terminus, applying dot blot, immunoblotting, immunoprecipitation and immunocytochemistry assays.
Browse additional application references in our FLAG® Literature portal."

Biochem/physiol Actions

FLAG epitope plays a crucial role in immunoaffinity purification of fusion proteins.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide

Preparation Note

Purified by affinity chromatography on a column bearing the immunizing peptide.

Legal Information

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

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Ryota Sato et al.
Frontiers in microbiology, 10, 1857-1857 (2019-08-29)
The envelope proteins of influenza A virus, hemagglutinin (HA) and neuraminidase (NA), play critical roles in viral entry to host cells and release from the cells, respectively. After protein synthesis, they are transported from the trans-Golgi network (TGN) to the
Makoto Miyazawa et al.
The Journal of biological chemistry, 286(22), 19191-19203 (2011-04-12)
The molecular chaperone prefoldin (PFD) is a complex comprised of six different subunits, PFD1-PFD6, and delivers newly synthesized unfolded proteins to cytosolic chaperonin TRiC/CCT to facilitate the folding of proteins. PFD subunits also have functions different from the function of
Martin S Taylor et al.
The Journal of biological chemistry, 288(45), 32211-32228 (2013-09-21)
Ghrelin O-acyltransferase (GOAT) is a polytopic integral membrane protein required for activation of ghrelin, a secreted metabolism-regulating peptide hormone. Although GOAT is a potential therapeutic target for the treatment of obesity and diabetes and plays a key role in other
Dorothee A Vogt et al.
PLoS pathogens, 9(4), e1003302-e1003302 (2013-04-18)
The nonstructural protein NS5A has emerged as a new drug target in antiviral therapies for Hepatitis C Virus (HCV) infection. NS5A is critically involved in viral RNA replication that takes place at newly formed membranes within the endoplasmic reticulum (membranous
Ecco Staller et al.
Journal of virology, 93(17) (2019-06-21)
ANP32 proteins have been implicated in supporting influenza virus replication, but most of the work to date has focused on the ability of avian Anp32 proteins to overcome restriction of avian influenza polymerases in human cells. Using a CRISPR approach

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