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Merck

A4596

ANTI-FLAG® M1 Agarose Affinity Gel

Synonym(s):

Anti-ddddk, Anti-dykddddk

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About This Item

NACRES:
NA.32
UNSPSC Code:
12352203
Conjugate:
agarose conjugate
Species reactivity:
-
Application:
Citations:
81
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conjugate

agarose conjugate

antibody product type

primary antibodies

form

suspension

isotype

IgG12b

capacity

≥0.6 mg/mL, gel binding capacity

storage temp.

−20°C

Quality Level

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

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Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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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.
E Di Zazzo et al.
TheScientificWorldJournal, 2014, 565839-565839 (2014-08-13)
Recent studies have shown that hyperinsulinemia may increase the cancer risk. Moreover, many tumors demonstrate an increased activation of IR signaling pathways. Phosphatidylinositol 3-kinase (PI3K) is necessary for insulin action. In epithelial cells, which do not express GLUT4 and gluconeogenic
Bo Zhou et al.
Journal of molecular endocrinology, 55(3), 231-243 (2015-09-17)
Progranulin (PGRN) has recently emerged as an important regulator for insulin resistance. However, the direct effect of PGRN in vivo and the underlying role of progranulin in adipose insulin resistance involving the autophagy mechanism is not fully understood. In this
Yong-Feng Han et al.
Cell research, 24(12), 1445-1465 (2014-11-26)
The SU(VAR)3-9-like histone methyltransferases usually catalyze repressive histone H3K9 methylation and are involved in transcriptional gene silencing in eukaryotic organisms. We identified a putative SU(VAR)3-9-like histone methyltransferase SUVR2 by a forward genetic screen and demonstrated that it is involved in
Fenju Lai et al.
Chinese journal of cancer, 31(9), 440-448 (2012-08-03)
A recently identified protein, FAN1 (FANCD2-associated nuclease 1, previously known as KIAA1018), is a novel nuclease associated with monoubiquitinated FANCD2 that is required for cellular resistance against DNA interstrand crosslinking (ICL) agents. The mechanisms of FAN1 regulation have not yet

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