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E2275

Sigma-Aldrich

pFLAG-CMV−6a,b,c Expression Vectors

set of pFLAG-CMV-6a, -6b, and -6c vectors for cytoplasmic expression of N-terminal FLAG

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About This Item

MDL number:
UNSPSC Code:
12352200

tag

FLAG® tagged

grade

for molecular biology

form

buffered aqueous solution

shipped in

dry ice

storage temp.

−20°C

General description

p-FLAG-CMV-6a, p-FLAG-CMV-6b, and p-FLAG-CMV-6c Expression Vectors used for the expression of N-terminal FLAG® tagged proteins in mammalian cells. pFLAG-CMV-6 a,b,c Expression Vectors are used as shuttle vectors for E. coli and mammalian cells. These vectors facilitate the intracellular expression of N-terminal FLAG-tagged fusion proteins. Transient expression in mammalian cells is driven by the CMV promoter-regulatory region. The SV40 origin of replication results in most efficient replication in mammalian cells expressing the SV40 large T antigen. The a, b, and c vector series makes all three reading frames available for every restriction site in the MCS.

Vector Maps and Sequences

Application

p-FLAG-CMV-6a, p-FLAG-CMV-6b, and p-FLAG-CMV-6c Expression Vectors are suitable for cytoplasmic expression of N-terminal FLAG® tagged proteins.

Components

  • p-FLAG-CMV-6a Expression Vector (20μg)
  • p-FLAG-CMV-6b Expression Vector (20 μg)
  • p-FLAG-CMV-6c Expression Vector (20 μg)
  • pFLAG-CMV-6a-BAP control plasmid (20 μg)

Legal Information

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

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Virginie W Gautier et al.
Proceedings of the National Academy of Sciences of the United States of America, 102(45), 16362-16367 (2005-11-02)
The primary function of the HIV-1 regulatory protein Tat, activation of transcription from the viral LTR, is highly regulated by complex interactions between Tat and a number of host cell proteins. Tat nuclear import, a process mediated by importin beta
Rick F Nelson et al.
The Journal of biological chemistry, 281(29), 20242-20251 (2006-05-10)
In SCF (Skp1/Cullin/F-box protein) ubiquitin ligases, substrate specificity is conferred by a diverse array of F-box proteins. Only in fully assembled SCF complexes, it is believed, can substrates bound to F-box proteins become ubiquitinated. Here we show that Fbx2, a

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