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Merck

CELLMM2

FLAG® M Purification Kit

For Mammalian expression systems.

Synonym(s):

Anti-ddddk, Anti-dykddddk

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About This Item

NACRES:
NA.32
UNSPSC Code:
12352200

Key Documents

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Product Name

FLAG® M Purification Kit, For Mammalian expression systems.

technique(s)

protein extraction: suitable

shipped in

wet ice

storage temp.

−20°C

Quality Level

200

Related Categories

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.

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

Kit Components Also Available Separately

Product No.
Description
SDS
  • C2978CelLytic™ M, Cell Lysis Reagent, Suitable for Mammalian cell lysis and protein solubilization.SDS
  • SAE0194Purified 3xFLAG® peptide, ≥95% (HPLC), lyophilized powderSDS
  • A2220ANTI-FLAG® M2 Affinity Gel, purified immunoglobulin, buffered aqueous glycerol solutionSDS
  • C2103Chromatography columns, general-purpose, volume 10 mL, Overall H 5 in.SDS

Storage Class

10 - Combustible liquids

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
128M4181V
11180736
087M4113V
11170303
106M4080V

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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
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
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
Weiming Xu et al.
Molecules (Basel, Switzerland), 17(10), 12086-12101 (2012-10-23)
Recent genetic studies have shown that PCSK9, one of the key genes in cholesterol metabolism, plays a critical role by controlling the level of low-density lipoprotein receptor. However, how PCSK9 mediates LDLR degradation is still unknown. By combining a shotgun
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