Kinases and Substrates
360 Recombinant Human Wild Type Kinases and additional 81 mutant forms, isoforms, or inactive forms are available right now. Each kinase construct is carefully selected from the literature, and the DNA sequence is confirmed prior to expression. We use different means to activate our kinases, e.g. co-expression with an upstream kinase, ATP treatment, or dephosphorylation.
Our quality control includes confirmation of amino acid sequence by peptide mass fingerprinting, checking the purity by SDS-PAGE, determination of concentration using Bradford, and determination of activity using substrates from our substrate library.
Further features of our kinases are: no lag phase activity, mostly GST-tagged, available from 5 µg sizes up to bulk amounts, batch-to-batch consistency.
The immobilization of target proteins onto sensor surfaces while maintaining both structure and activity have been problematic and rate-limiting for the acquisition of meaningful SPR and/or BLI data in small molecule drug discovery. Consequently, Carna Biosciences developed a technology to produce site-specific Biotinylated Kinases in order to provide an easy-to-use solution in the SPR technology for kinase inhibitor evaluation. During expression, biotin is added in vivo. The kinase domain is not affected and maintains its kinase activity and structure.
Features of our Biotinylated Kinases are: Biotinylation at a single site outside of the catalytic domain, enzymatic activity of the kinase and structure are retained, biotinylated kinases highly purified by affinity chromatography, applicable to various binding assays using avidin-biotin interaction, such as SPR or TR-FET assays.
New BTN-Kinases: BTN-FLT3[non-activated], BTN-PI3KCA[E542K]/PIK3R1, BTN-PIK3CA[E545K]/PIK3R1