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TP0010

Millipore

FLAG® HA Tandem Affinity Purification Kit

Synonym(s):

Anti-ddddk, Anti-dykddddk

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

General description

TAP technology is a recent development in protein purification. This technology incorporates tandem-linked affinity tags into genes of interest so that high purity fusion proteins can be isolated through two consecutive affinity purification steps. The technology is particularly useful for the isolation and identification of protein complexes by adding a tandem affinity tag to a known "bait" protein to pull down endogenous proteins that interact with the targeted protein of interest.

Application

The FLAG® HA Tandem Affinity Purification Kit is designed for the isolation of high purity FLAG-HA dual-tagged fusion proteins from complex matrix, such as cell lysates and tissue homogenates. The kit is particularly suitable for isolation of protein complexes using TAP (Tandem Affinity Purification) technology.

Sutitable for mass spectrometry analysis and western blotting.

Learn more product details in our FLAG® application portal.

Legal Information

FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

Kit Components Also Available Separately

Product No.
Description
SDS
  • F2426EZview™ Red ANTI-FLAG® M2 Affinity Gel, clone M2SDS
  • A2095Monoclonal Anti-HA−Agarose antibody produced in mouse, clone HA-7, purified immunoglobulin, PBS suspensionSDS
  • R0278RIPA BufferSDS
  • F47993X FLAG® Peptide, lyophilized powderSDS
  • U4883Urea, 8 M (after reconstitution with 16 mL high purity water)SDS

pictograms

Exclamation markEnvironment
GHS07,GHS09

signalword

Warning

hcodes

H319,H411

Hazard Classifications

Aquatic Chronic 2 - Eye Irrit. 2

Storage Class

10 - Combustible liquids

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Junsong Zhang et al.
Journal of virology, 90(8), 3966-3980 (2016-02-05)
The viral ribonucleoprotein (vRNP) complex of influenza A viruses (IAVs) contains an RNA-dependent RNA polymerase complex (RdRp) and nucleoprotein (NP) and is the functional unit for viral RNA transcription and replication. The vRNP complex is an important determinant of virus
Wei Li et al.
Cell, 140(4), 477-490 (2010-02-25)
Current models imply that the FERM domain protein Merlin, encoded by the tumor suppressor NF2, inhibits mitogenic signaling at or near the plasma membrane. Here, we show that the closed, growth-inhibitory form of Merlin accumulates in the nucleus, binds to
Karthik Ramachandran et al.
iScience, 25(1), 103722-103722 (2022-01-11)
SARS-CoV-2 is a newly identified coronavirus that causes the respiratory disease called coronavirus disease 2019 (COVID-19). With an urgent need for therapeutics, we lack a full understanding of the molecular basis of SARS-CoV-2-induced cellular damage and disease progression. Here, we
Kosei Sato et al.
Nature communications, 10(1), 166-166 (2019-01-13)
In Drosophila, some neurons develop sex-specific neurites that contribute to dimorphic circuits for sex-specific behavior. As opposed to the idea that the sexual dichotomy in transcriptional profiles produced by a sex-specific factor underlies such sex differences, we discovered that the

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