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P2983

Millipore

ANTI-FLAG® High Sensitivity, M2 coated 96-well plates

96-well, clear, polystyrene, flat bottom plate

Synonym(s):

Monoclonal ANTI-FLAG® M2 antibody produced in mouse, Anti-ddddk, Anti-dykddddk

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.32

antibody product type

primary antibodies

Quality Level

200

material

polystyrene

clone

monoclonal

shelf life

Unopened plates are stable for 2 years. Once opened they are stable for 2 weeks.

technique(s)

ELISA: suitable

isotype

IgG1

capacity

100-300 ng/well

storage temp.

2-8°C

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General description

The Anti-FLAG® HS, M2 Coated Plates are designed to ensure a higher binding capacity than other plates. This is due to the orientation of the Anti-FLAG® M2 mouse monoclonal IgG1 antibody on the plates. The antibody is covalently linked to the surface of a microtiter plate via the Fc portion of the antibody.

Application

ANTI-FLAG® High Sensitivity, M2 coated 96-well plates is used for Enzyme-linked immunosorbent assays. A convenient, ready to use, platform for the capture and detection of FLAG® fusion proteins. The ANTI-FLAG® M2 antibody is covalently attached to the surface through the Fc portion and can detect 1 ng FLAG fusion protein/well with a capacity of up to 300ng/well. Suitable for screening for expression, study of protein:protein interactions and ELISA assays. Manufactured under ISO 9002 in Sigma′s GMP facility, ANTI-FLAG®P2983 high sensitivity M2 coated multiwell plates utilize a flat bottom, polystyrene baseplate.

Learn more product details in our FLAG® application portal.

Storage and Stability

Once plates are opened, they should be stored with desiccant at 2- 8 °C and used within two weeks.

Other Notes

Components:
The plate is supplied as a 96-well microtiter plate with clear sides and bottom.
Coating:
ANTI-FLAG® M2 mouse monoclonal antibody, IgG1, is coated at a reaction volume of 200 ml/well.
Blocking:
The wells are pre-blocked for convenience at 275 to 300 ml/well with a complex solution containing bovine serum albumin.
Specificity:
The plates are specific for the FLAG epitope regardless of its placement in the fusion protein: amino-terminal, Met-amino terminal, carboxy terminal or internal. Binding of the epitope is not Ca2+ dependent.
Sensitivity:
Detection of 1 ng/well of a control fusion protein was observed in an ELISA format with p-Nitrophenyl Phosphate (pNPP) as a substrate.
Capacity:
Capture of 100 to 300 ng/well of a FLAG fusion protein has been demonstrated.

Legal Information

ANTI-FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
F-127 is a registered trademark of BASF SE
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

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Natalie F Shanks et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 34(36), 12104-12120 (2014-09-05)
Cornichon homologs (CNIHs) are AMPA-type glutamate receptor (AMPAR) auxiliary subunits that modulate AMPAR ion channel function and trafficking. Mechanisms underlying this interaction and functional modulation of the receptor complex are currently unclear. Here, using proteins expressed from mouse and rat
Molecular dissection of the interaction between the AMPA receptor and cornichon homolog-3.
Shanks NF, Cais O, Maruo T, et al.
The Journal of Neuroscience, 34(36), 12104-12120 (2014)
Qiongming Liu et al.
BMC biotechnology, 10, 78-78 (2010-10-29)
Analysis of protein-protein interactions (PPIs) is a valuable approach for the characterization of huge networks of protein complexes or proteins of unknown function. Co-immunoprecipitation (coIP) using affinity resins coupled to protein A/G is the most widely used method for PPI
Shu Kachi et al.
Human gene therapy, 20(1), 31-39 (2009-01-01)
Equine infectious anemia virus (EIAV) is a nonprimate lentivirus that does not cause human disease. Subretinal injection into mice of a recombinant EIAV lentiviral vector in which lacZ is driven by a CMV promoter (EIAV CMV LacZ) resulted in rapid
FLAG 96-well Immunoprecipitation System for High-Throughput Protein-Protein Interaction Studies
Uder, S., et al.
Molecular Biology, 4 null
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