Recombinant human CLK1 (129–end) was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. CLK1, also known as STY, is a member of the CDC2-like (or LAMMER) family of dual specificity protein kinases. The phosphorylated serine/arginine-rich (SR) proteins are involved in the pre-mRNA processing and releasing through nucleus into nucleoplasm. CLK1, which could phosphorylate the specific SR proteins (1) such as ASF/SF2, may directly regulate the activity and compartmentalization of SR splicing factors (2).
ADP-Glo™ Kinase Assay is a luminescent kinase assay that measures ADP formed from a kinase reaction; ADP is converted into ATP, which is a substrate in a reaction catalyzed by Ultra-Glo™ Luciferase that produces light. The luminescent signal positively correlates with ADP amount and kinase activity. The assay is well suited for measuring the effects chemical compounds have on the activity of a broad range of purified kinases, making it ideal for both primary screening as well as kinase selectivity profiling. The ADP-Glo™ Kinase Assay can be used to monitor the activity of virtually any ADP-generating enzyme (e.g., kinase or ATPase) using up to 1mM ATP.
Profile More Compounds In-House: ADP-Glo™ Kinase Assay + Kinase Enzyme System is optimized so that you are up and running in no time. Complete Systems: The Kinase Enzyme Systems include a recombinant kinase enzyme, a substrate appropriate for the enzyme, a reaction buffer, DTT and supplemental reagents as needed. Obtain Reliable Results: The broad dynamic range, the ease of use and better sensitivity obtained with ADP-Glo™ Kinase Assay result in less ambiguous data.
Notes
Kinase Enzyme System manufactured by SignalChem.
Bulk quantities available upon request.
References
1.Prasad J. et al. (2003) Regulation and substrate specificity of the SR protein kinase Clk/Sty. Mol. Cell Biol. 23, 4139–49.
2.Colwill, K. et al. (1996) SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors. J. Biol. Chem. 271, 24569–75.