BellBrook Labs Transcreener® ADP2 Assay
BellBrook Labs Transcreener ADP2 Assays are homogenous assays with fluorescent readouts that enable the facile detection and screening of established drug targets including protein and lipid kinases as wells as emerging targets such as carbohydrate kinases, tryphosphatases, heat shock proteins and other ATPases. The Bell Brook Labs ADP2 assay is based on the immunodetection of ADP and allows the screening of diverse enzymes with native and synthetic substrates, or enzymes with intrinsic ATPase (no substrate) – all with the same set of reagents.
THREE DETECTION MODES:
• Fluorescence Polarization (FP)
• Time-Resolved Forster-Resonance Energy Transfer (TR-FRET)
• Fluorescence Intensity (FI)
To accommodate the variety of instrument and detection format preferences expressed by BellBrook lab customers, BellBrook Labs have expanded the Transcreener ADP2 Assay product line to include three fluorescent detection formats, all with emission in the red region of the visible spectrum to minimize compound interference. All three assays share the same qualities of assay sensitivity and ease of use. Whether you are doing assay development, screening, or hit to lead activities, there is a Transcreener ADP2 Assay that is right for you
Features of BellBrook Labs Transcreener ADP2 Assay:
• New EZ Protocol
• Increased Sensitivity
• Use Less Enzyme
• Screen Low Specific Activity Enzymes
• Excellent Z' Values at Initial Enzyme Velocity Kinetics
• Miniaturize to 1536
• Robust Performance on Industry-Standard Microplate Readers
The Bell Brook Labs Transcreener ADP2 FP Assay is a new assay, with greater sensitivity than the original BellBrook Lab Transcreener ADP Assay. The improvement is a more sensitive antibody against ADP yielding an excellent signal at less than or equal to 10% ATP consumption for a broad range of initial ATP concentrations (0.1-1,000 μM). The result is the ability to screen low ATP Km enzymes, and to use initial velocity enzyme kinetics at or below ATP Km concentrations, which leads to accurate inhibitor potencies and the ability to use less enzyme and substrate. Ratiometric, red-shifted fluorescence polarization output minimizes signal variability and reduces compound interference, resulting in robust Z´ values ≥ 0.7 in 384 and 1536-well formats.