Recombinant full-length human KHS1 was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. KHS1 belongs to the serine/threonine kinase family that has a STE20-like protein kinase domain, which stimulates the stress-activated protein kinase (SAPK, also known as Jun kinase or JNK) pathway (1). It is a mitogen-activated protein kinase kinase kinase kinase 5, termed germinal center kinase related (GCKR). Recently, the KH domain of Escherichia coli polynucleotide phosphorylase has been reported to be necessary for autoregulation and growth at low temperature (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.Shi, C.S. et al. (1999) TNF-mediated activation of the stress-activated protein kinase pathway: TNF receptor-associated factor 2 recruits and activates germinal center kinase related. J. Immunol. 163, 3279–85.
2.Maura Epifanía, M.O. et al. (2007) The KH and S1 domains of Escherichia coli polynucleotide phosphorylase are necessary for autoregulation and growth at low temperature. Biochim. et Biophy. Acta (BBA) 1769, 194–203.