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Merck

CELLMM2

FLAG® M Purification Kit

For Mammalian expression systems.

Synonyme(s) :

Anti-ddddk, Anti-dykddddk

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A propos de cet article

NACRES:
NA.32
UNSPSC Code:
12352200
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Nom du produit

FLAG® M Purification Kit, For Mammalian expression systems.

technique(s)

protein extraction: suitable

shipped in

wet ice

storage temp.

−20°C

Quality Level

Packaging

Sufficient for 3-5 uses of 1-ml affinity purification column.

Legal Information

ANTI-FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
CelLytic is a trademark of Sigma-Aldrich Co. LLC
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

Application

The FLAG Purification Kit utilizes CelLytic Reagents for rapid and efficient cell lysis and protein extraction and ANTI-FLAG® M2 affinity gel for affinity purification of active FLAG fusion proteins.

Learn more product details in our FLAG® application portal.

Features and Benefits

  • Includes ready to use reagents, columns, and a detailed protocol for affinity purification of FLAG fusion proteins.
  • ANTI-FLAG M2 Affinity Gel allows efficient binding of FLAG fusion proteins without the need for preliminary steps and calibrations.
  • Two alternatives for efficient elution conditions (by acidic conditions or by competition with FLAG peptide).

Other Notes

Kit contains CelLytic™ M for cell lysis and protein extraction from Mammalian cells.

Composants de kit également disponibles séparément

Réf. du produit
Description
FDS

  • C2978CelLytic M, Cell Lysis Reagent, Suitable for Mammalian cell lysis and protein solubilization.FDS

  • SAE0194Purified 3xFLAG® peptide, ≥95% (HPLC), lyophilized powderFDS

  • A2220ANTI-FLAG® M2 Affinity Gel, purified immunoglobulin, buffered aqueous glycerol solutionFDS

  • C2103Chromatography columns, general-purpose, volume 10 mL, Overall H 5 in.FDS

Classe de stockage

10 - Combustible liquids


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Consulter la Bibliothèque de documents

Severa Bunda et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(36), E3785-E3794 (2014-08-27)
Mutations in Ras GTPase and various other components of the Ras signaling pathways are among the most common genetic alterations in human cancers and also have been identified in several familial developmental syndromes. Over the past few decades it has
Amitava Mukherjee et al.
PLoS pathogens, 7(3), e1001311-e1001311 (2011-03-26)
The host innate immune response to viral infections often involves the activation of parallel pattern recognition receptor (PRR) pathways that converge on the induction of type I interferons (IFNs). Several viruses have evolved sophisticated mechanisms to attenuate antiviral host signaling
Erik G Puffenberger et al.
PloS one, 7(1), e28936-e28936 (2012-01-27)
The Clinic for Special Children (CSC) has integrated biochemical and molecular methods into a rural pediatric practice serving Old Order Amish and Mennonite (Plain) children. Among the Plain people, we have used single nucleotide polymorphism (SNP) microarrays to genetically map
Takeshi Into et al.
Molecular and cellular biology, 28(4), 1338-1347 (2007-12-19)
Nitric oxide (NO) has been thought to regulate the immune system through S nitrosylation of the transcriptional factor NF-kappaB. However, regulatory effects of NO on innate immune responses are unclear. Here, we report that NO has a capability to control
M D Mostaqul Huq et al.
Molecular & cellular proteomics : MCP, 6(4), 677-688 (2007-01-09)
Retinoic acid receptors (RARs) belong to the nuclear receptor superfamily. The mechanism of ligand-dependent activation of RARs is well known. The effect of protein phosphorylation on the activity of RARs has also been demonstrated. However, it is unclear whether other

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