Skip to Content
Merck
All Photos(4)

Documents

F7425

Millipore

ANTI-FLAG® antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-ddddk, Anti-dykddddk

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.32

biological source

rabbit

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

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.
Learn more product details in our FLAG® application 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

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
Gouji Toyokawa et al.
Neoplasia (New York, N.Y.), 13(10), 887-898 (2011-10-27)
A number of histone methyltransferases have been identified and biochemically characterized, but the pathologic roles of their dysfunction in human diseases like cancer are not well understood. Here, we demonstrate that Wolf-Hirschhorn syndrome candidate 1 (WHSC1) plays important roles in

Related Content

Protein and nucleic acid interaction reagents and resources for investing protein-RNA, protein-DNA, and protein-protein interactions and associated applications.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service