Member since: 2015
Organization: EMD Serono
Application Area: Kinetic profiling
"The ADP2 assay is a great choice for measuring activity for any ADP-generating enzyme in both real time and endpoint formats. The universal detection system has been very useful for more challenging targets in our lab."
Member since: 2007
Organization: Eli Lilly Co
"Excellent blend of simplicity, economics & good science. Excellent technical support."
BellBrook Labs Transcreener ADP2 Kinase Assays are homogeneous assays with fluorescent readouts that enable the easy 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:
To accommodate the variety of instrument and detection format preferences expressed by BellBrook lab customers, BellBrook Labs have expanded the Transcreener ADP 2 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 ADP 2 Assay that is right for you.
Features of BellBrook Labs Transcreener ADP2 Assay:
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.