DB MiniKinase Panel™: We select 48 kinases for you to represent the whole kinome

(DB-MiniKinase-panel)

The DB MiniKinase Panel™ is a curated set of 48 kinase assays designed to provide the most efficient representation of the human kinome. By analyzing the inhibition "fingerprints" of 72 inhibitors across 257 kinases, we used a proprietary optimization algorithm to select the most representative set of assays. This allows you to cover the broadest possible inhibition profile space with just 48 targets, making it an indispensable, cost-effective tool for rapid compound profiling and lead discovery.


Download the DB MiniKinase Panel™ assay list here!


Download the full DIANA Kinase Inhibitor Profiling booklet here!

DIANA Technology Features

DIANA Technology: DIANA is patented solid-phase competitive binding assay that uniquely combines small molecule-based DIANA probes with the strengths of ELISA and qPCR.

Quantitative Results: Determination of quantitative potency data (Kd) from each measurement thanks to the proprietary DIANA technology.

Affordable Excellence: Our service has fast turnaround time and it is possible to fully customize the order. Finally, the pricing makes our top-tier solution accessible to everyone.

Internal Quality Control – Binding potency of known inhibitor is determined for each kinase

Service Information

Name

No. of kinases

Cpds

Price (EUR)

Price per kinase (EUR)

Turnaround time**

Result

DB MiniKinase Panel™

48

1

960

20

7 business days

Kd

DB MiniKinase Panel™

48

2

1440

15*

7 business days

Kd

*Price is applicable for all orders which profile more than 2 compounds.

**Counts from the day compounds are delivered to our testing facility. For complex orders the turnaround time can be extended to 14 business days.

Prices exclude VAT

Materials to download

Document name

Download

DIANA Kinase Inhibitor Profiling: Booklet

Download

2-D representation of the kinase inhibition “fingerprint” space using UMAP algorithm

DB MiniKinase Panel™ algorithm of kinome representation:Kd values for the interactions of 257 human kinases with 72 kinase inhibitors were retrieved from publicly available resources. Interactions where no Kd value was measured were assigned a Kd value of 10 μM. The Kd values were then converted to their decadic logarithms and the distance dij was calculated for each pair of kinases i and j as the Euclidean distance between the respective log10 Kd value vectors. The distances dij were subsequently normalized to the range <0.0, 1.0> by dividing each distance by the maximum of all distances found, and converted to a similarity sij by the transformation sij = 1.0 – normalized dij. A ranking of the kinases was finally generated by subjecting the similarity matrix S with elements sij to a naive facility location selection algorithm. The distances dij were also used for the preparation of low (2)-dimensional representations of the kinase space using the UMAP algorithm (see graphs below).

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