Skip to Content
MilliporeSigma

A4596

Millipore

ANTI-FLAG® M1 Agarose Affinity Gel

Synonym(s):

Anti-ddddk, Anti-dykddddk

Sign Into View Organizational & Contract Pricing

Select a Size


About This Item

UNSPSC Code:
12352203
NACRES:
NA.32
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

conjugate

agarose conjugate

Quality Level

antibody product type

primary antibodies

form

suspension

isotype

IgG12b

capacity

≥0.6 mg/mL, gel binding capacity

storage temp.

−20°C

General description

ANTI-FLAG® M1 Agarose Affinity Gel is a purified IgG2B monoclonal antibody covalently attached to agarose.

Application

For purification of N-terminal FLAG fusion proteins. Since binding is Ca2+-dependent, proteins can be eluted with a buffer containing EDTA, as well as by the standard methods using either FLAG peptide or glycine-HCl buffer, pH 3. ANTI-FLAG M1 does not bind to Met-FLAG fusion proteins, so this resin is not appropriate for purifying unprocessed, cytoplasmically expressed fusion proteins.

Affinity gel is for calcium mediated purification of N-terminal FLAG fusion proteins.

immunoprecipitation (IP): suitable

Elution - FLAG peptide, Glycine, pH 3.5 EDTA

Learn more product details in our FLAG® application portal.

Biochem/physiol Actions

Binding specificity: Free N-Terminus of FLAG sequence
N-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-C

Features and Benefits

  • Typically purify fusion proteins from crude lysates to single band purity in just one chromatography step.
  • Fusion protein may be eluted from affinity resin by mild elution with EDTA.
  • A solution of FLAG peptide can be used for gentle, non-denaturing elution of FLAG fusion proteins.

Physical form

Suspension of beaded agarose in 50% glycerol containing 10 mM sodium phosphate, 150 mM NaCl, pH 7.4, 0.02% (w/v) sodium azide

Other Notes

ANTI-FLAG® M1 does not bind to Met-FLAG fusion proteins, so this resin is not appropriate for purifying unprocessed, cytoplasmically expressed fusion proteins.

Legal Information

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

Not finding the right product?  

Try our Product Selector Tool.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

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

Visit the Document Library

Ai Lu et al.
Biochemical and biophysical research communications, 513(3), 746-752 (2019-04-17)
Phosphoribosylformylglycinamidine synthase (PFAS) is an essential enzyme in de novo synthesis of purine. Previously, PFAS has been reported to modulate RIG-I activation during viral infection via deamidation. In this study, we sought to identify potential substrates that PFAS can deamidate.
Weinan Zheng et al.
Cell reports, 27(6), 1875-1885 (2019-05-09)
Naproxen is a non-steroidal anti-inflammatory drug that has previously been shown to exert antiviral activity against influenza A virus by inhibiting nucleoprotein (NP) binding to RNA. Here, we show that naproxen is a potential broad, multi-mechanistic anti-influenza virus therapeutic, as
Carol S Bookwalter et al.
The Journal of biological chemistry, 292(47), 19290-19303 (2017-10-06)
Motility of the apicomplexan malaria parasite Plasmodium falciparum is enabled by a multiprotein glideosome complex, whose core is the class XIV myosin motor, PfMyoA, and a divergent Plasmodium actin (PfAct1). Parasite motility is necessary for host-cell invasion and virulence, but
Kengo Okamoto et al.
Oncotarget, 10(46), 4743-4760 (2019-08-16)
Triple-negative breast cancer (TNBC) is very aggressive and lacks specific therapeutic targets. Ribosome RNAs (rRNAs) are central components of ribosomes and transcribed in nucleoli, and the level of rRNA transcription greatly affects ribosome production and cell proliferation. We have reported
Jin-Kwang Kim et al.
Molecular cell, 68(4), 698-714 (2017-11-18)
Telomere elongation through telomerase enables chromosome survival during cellular proliferation. The conserved multifunctional shelterin complex associates with telomeres to coordinate multiple telomere activities, including telomere elongation by telomerase. Similar to the human shelterin, fission yeast shelterin is composed of telomeric

Related Content

Protein expression technologies for various expression systems supporting research, therapeutics, and vaccine production.

Protein purification techniques, reagents, and protocols for purifying recombinant proteins using methods including, ion-exchange, size-exclusion, and protein affinity chromatography.

Tecnologías de expresión de proteínas para varios sistemas de expresión que propician la investigación, la terapéutica y la producción de vacunas.

See All

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