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Merck
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A4596

Millipore

ANTI-FLAG® M1 Agarose Affinity Gel

Sinónimos:

Anti-ddddk, Anti-dykddddk

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.32

conjugate

agarose conjugate

Quality Level

200

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.

Specificity

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

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.

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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Referencia del producto
Descripción
Precios

92210

Timestrip Plus™ 0 °C

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
Hang Zhou et al.
EMBO molecular medicine, 11(3) (2019-02-20)
Arthrogryposis is a group of phenotypically and genetically heterogeneous disorders characterized by congenital contractures of two or more parts of the body; the pathogenesis and the causative genes of arthrogryposis remain undetermined. We examined a four-generation arthrogryposis pedigree characterized by
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