Skip to Content
Merck

Key Documents

View All Documentation

A2220

ANTI-FLAG® M2 Affinity Gel

purified immunoglobulin, buffered aqueous glycerol solution

Synonym(s):

Monoclonal ANTI-FLAG® M2, ANTI-FLAG® M2 Affinity Agarose Gel, Anti-ddddk, Anti-dykddddk

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View

About This Item

NACRES:
NA.32
UNSPSC Code:
12352203
Conjugate:
agarose conjugate
Clone:
M2, monoclonal
Application:
IP, affinity chromatography
Citations:
1232
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

conjugate

agarose conjugate

Quality Level

200

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M2, monoclonal

form

buffered aqueous glycerol solution

analyte chemical class(es)

proteins

technique(s)

affinity chromatography: suitable, immunoprecipitation (IP): suitable

matrix

(4% agarose bead; 45-165μm bead size)

isotype

IgG1

capacity

>0.6 mg/mL, resin binding capacity (FLAG-BAP)

shipped in

wet ice

storage temp.

−20°C

General description

Anti-FLAG M2 Affinity gel is a mouse monoclonal antibody that is covalently attached to agarose. The antibody binds FLAG at the N-terminal, Met-N-terminal, C-terminal and internal locations of fusion proteins. Binding is calcium-independent.

Elution - FLAG® peptide, Glycine, pH 3.5, 3x FLAG® peptide
FLAG® peptide, Glycine, pH3.5, 3x FLAG® peptide

Immunogen

DYKDDDDK

Application

Anti-FLAG® M2 affinity gel has been used for western blotting, immunoprecipitation and for the purification of FLAG fusion proteins.

Learn more product details in our FLAG® application portal.

Physical form

Suspension in buffered saline containing azide as preservative and 50% glycerol

Other Notes

2024 CiteAb Award Winner for Supplier Succeeding in Parkinson′s Research

Legal Information

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

Disclaimer

FLAG® tag, 3x FLAG®, DYKDDDDK tag

Still not finding the right product?

Try our Product Selector Tool to narrow your options

Storage Class

10 - Combustible liquids

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
0000296512
0000278651
0000278652
078K60021
108K6016

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.

Search for a COA

Already Own This Product?

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

Visit the Document Library

Related Content

Product Information Sheet - A2220
EZview Red Protein A and ANTI-FLAG M2 Affinity Gels

EZviewTM Red Protein A and ANTI-FLAG® M2 Affinity Gels: Immunoprecipitation with Enhanced Visibility Affinity Beads - Technical Article - July 2001

Nora Nonne et al.
Nucleic acids research, 38(4), e20-e20 (2009-12-04)
MicroRNAs (miRNAs) bind to Argonaute proteins, and together they form the RISC complex and regulate target mRNA translation and/or stability. Identification of mRNA targets is key to deciphering the physiological functions and mode of action of miRNAs. In mammals, miRNAs
Yu Ti Cheng et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(35), 14694-14699 (2011-08-30)
The nucleotide-binding domain and leucine-rich repeats containing proteins (NLRs) serve as immune receptors in both plants and animals. Overaccumulation of NLRs often leads to autoimmune responses, suggesting that the levels of these immune receptors must be tightly controlled. However, the
William G Roach et al.
The Biochemical journal, 403(2), 353-358 (2007-02-06)
Insulin stimulation of the trafficking of the glucose transporter GLUT4 to the plasma membrane is controlled in part by the phosphorylation of the Rab GAP (GTPase-activating protein) AS160 (also known as Tbc1d4). Considerable evidence indicates that the phosphorylation of this
View All Related Papers