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LANCE® Eu-W1024 phospho-(Ser) 14-3-3 binding motif antibody, 10 µg

Europium-labeled anti-phospho-(Ser) 14-3-3 motif antibody, for use in LANCE® TR-FRET kinase assays.

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Detail Information

Phospho-14-3-3 binding motif antibody is an affinity-purified rabbit polyclonal antibody (supplied by Cell Signaling Technology). It detects phosphorylated 14-3-3 binding proteins which contain phosphorylated serine surrounded by proline at the +2 position and arginine or lysine at the -3 position. It weakly cross-reacts when phospho-threonine replaces phospho-serine in this motif. The antibody also recognizes the motif containing phospho-serine surrounded by phenylalanine at the +1 position and arginine at the -3 position. Binding is phospho-specific and largely independent of the surrounding amino acid sequence.

LANCE® (Lanthanide chelate excite) and LANCE® Ultra are our TR-FRET (time-resolved fluorescence resonance energy transfer), homogeneous (no wash) technologies. One molecule of interest is labeled with a donor fluorophore (a LANCE Europium chelate) and the second molecule is labeled with an acceptor fluorophore [ULight™ dye, allophycocyanin (APC), etc.]. Upon excitation at 320 or 340 nm, energy can be transferred from the donor Europium chelate to the acceptor fluorophore if sufficiently close for FRET (~10 nm). This results in the emission of light at 665 nm (for ULight dye and APC).


Antibody Conjugates Anti-P-Ser 14-3-3
Automation Compatible Yes
Detection Method Time-Resolved Fluorescence (TRF), TR-FRET
Experimental Type In vitro
Fluorophore Eu-W1024
Molecular Modification Phosphorylation
Product Brand Name LANCE
Shipping Condition Blue Ice
Unit Size 10 µg
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Application Note

Measurement of p38/MAPK Activity Using LANCE

Protein kinases regulate several important functions within cells including metabolism, cell cycle progression, angiogenesis, cell adhesion, etc. Specifically, mitogen-activated protein kinases (MAPK) play a central role in the cellular response to environmental stress, growth factors, and cytokines.

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