LANCE Ultra Tau-Ser400 O-GlcNAc hydrolase (OGA) Assay

T E C H N I C A L
N O T E
U-TRF #49
LANCE Ultra Tau-Ser400 O-GlcNAc
hydrolase (OGA) Assay
Marie-Élaine Caruso
Mireille Caron
Nancy Gauthier
Anja Rodenbrock
Philippe Bourgeois
Liliana Pedro
Lucille Beaudet
Roberto Rodriguez-Suarez
LANCE® Ultra TR-FRET Technology
PerkinElmer, Inc.
Montreal, QC
Canada H3J 1R4
This LANCE Ultra immunodetection assay measures the hydrolysis of an O-GlcNAc moiety
from a biotinylated Tau-Ser400-O-GlcNAc peptide.
LANCE Ultra Europium-anti-O-linked-GlcNAc Antibody:
• TRF0413-D: 10 µg, 1,562 assay points*
• TRF0413-M: 100 µg, 15,625 assay points*
*6.7 fmol/assay point
Peptide Sequence:
KWKHGAEIVYKSPVV-S(O-GlcNAc)-GDTSPRHLSNVK-K(biotin)-NH2
GlcNac
B
S/T
No
Enzyme
+ O-GlcNAc
Hydrolase
GlcNac
B
S/T
B
S/T
+ Eu-Ab
+ ULight-SA
+ Eu-Ab
+ ULight-SA
FRET
Eu
Excitation
320 or 340 nm
No FRET
Eu
GlcNac
ULight
B
S/T
ULight
B
S/T
Em 665 nm
Figure 1. Schematic representation of the LANCE Ultra detection
of an O-GlcNAcylated peptide (B: biotin group; S/T: serine or threonine residue).
Excitation
320 or 340 nm
LANCE Ultra Assays
LANCE Ultra time-resolved fluorescence resonance energy
transfer (TR-FRET) assays use a proprietary europium
chelate donor dye, W1024 (Eu), together with ULight™, a
small molecular weight acceptor dye with a red-shifted
fluorescent emission. In this technical note, we present
the optimization of an OGA signal-decrease assay using
as substrate a biotinylated Tau-derived peptide
O-GlcNAcylated at Ser400. In this assay, detection of the
non-hydrolyzed O-GlcNAcylated substrate was performed
by the addition of the Eu-labeled antibody (Eu-Ab) and
ULight-Streptavidin (ULight-SA), which bring the Eu donor
and ULight acceptor dye molecules into close proximity.
Upon irradiation at 320 or 340 nm, the energy from the
Eu donor is transferred to the ULight acceptor dye which,
in turn, generates light at 665 nm. The signal decrease is
proportional to the activity of the OGA enzyme.
Development of a LANCE Ultra Tau-Ser400 O-GlcNAc
hydrolase (OGA) Assay
Experiment 1: Enzymatic Titration and Time-Course
Reagents needed for this assay:
Europium-anti-O-linked-GlcNAc Antibody
PerkinElmer # TRF0413
LANCE Ultra ULight-Streptavidin
PerkinElmer # TRF0102
Tau-Ser400-O-GlcNAc (388-411), biotinylated
AnaSpec # 65409
LANCE Detection Buffer, 10X
PerkinElmer # CR97-100
O-GlcNAcase (S. pyogenes), recombinant (OGA)
Prozomix # PRO-E0255
White opaque OptiPlate™-384
PerkinElmer # 6007290
TopSeal -A film
PerkinElmer # 6050195
O-(2-Acetamido-2-deoxy-D-glucopyranosylidene)
amino N-phenyl carbamate (PUGNAc)
Carbosynth # EA06838
N6-Methyladenine
Carbosynth # FM10151
™
Assay buffer: 20 mM MES, pH 6, 0.05% BSA and 0.01% Tween
Enzymatic progress curves were performed by incubating OGA at concentrations
ranging from 0.125 to 3 nM with 250 nM biotinylated Tau-Ser400-O-GlcNAc
peptide substrate. Detection Mix was added to stop the reactions at the indicated
times and signal was read after 60 min. A 60 min reaction time using 1 nM
enzyme was selected for all subsequent experiments.
Experiment 2: Enzyme Inhibition
Standard Protocol
• Dilute OGA, inhibitors and biotinylated biotinylated Tau-Ser400-O-GlcNAc
peptide substrate in Assay Buffer just before use.
• Add to the wells of a white OptiPlate-384:
– 2.5 µL of inhibitor (4X) or Assay Buffer
– 2.5 µL of enzyme (4X)
– Incubate for 5 min at room temperature (RT).
– 5.0 µL biotinylated Tau-Ser400-O-GlcNAc peptide (2X)
• Cover the plate with TopSeal-A film and incubate at RT.
• Prepare Detection Mix by diluting the Eu-Ab to 0.67 nM and
ULight-Streptavidin to 100 nM in 1X LANCE Detection Buffer (final
concentrations of 0.33 nM and 50 nM in 20 µL total assay volume).
• Add 10 µL of Detection Mix. Addition of the Detection mix will stop the
enzymatic reactions.
Serial dilutions of PUGNAc and N6-Methyladenine ranging from 100 pM to
10 µM and 10 nM to 1 mM, respectively, were pre-incubated for 5 min with
1 nM OGA. Enzymatic reactions were initiated by the addition of 250 nM
biotinylated Tau-Ser400-O-GlcNAc peptide substrate. Enzymatic reactions
contain 1% DMSO.
Experiment 3: Z’-factor Determination
• Cover with TopSeal-A film and incubate 60 min at RT.
• Remove the TopSeal-A film and read signal with the EnVision® Multilabel
Plate Reader in TR-FRET mode (excitation at 320 or 340 nm and emission
at 665 nm).
OGA (1 nM) was pre-incubated with or without 1 µM PUGNAc or 250 µM
N6-Methyladenine for 5 min. Enzymatic reactions were initiated by the addition
of 250 nM biotinylated Tau-Ser400-O-GlcNAc peptide substrate. Enzymatic
reactions contain 1% DMSO.
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010816_01
Printed in USA
Dec. 2012