Full-length recombinant human CAMK1γ was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. CAMK1γ (CLICK-III), a member of CAMK family, is a novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein kinase. Full activation of CaMK1γ requires both Ca2+/CaM and phosphorylation by CAMKK. CAMK1γ transcript is most abundant in neurons, with the highest levels in limited nuclei such as the central nucleus of the amygdala (CeA) and the ventromedial hypothalamus (1).
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.
Kinase Enzyme System contains:
Kinase: CAMK1γ, 10μg (Human, recombinant full-length). MW: ~80kDa. Substrate: Autocamtide 2 peptide (KKALRRQETVDAL-amide); derived from the autophosphorylation site (amino acids 283–290) on CaMKII. Other: Reaction Buffer, DTT, Ca2+/Calmodulin Solution.
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.Takemoto-Kimura, S. et al. (2003) Molecular cloning and characterization of CLICK-III/CaMKIgamma, a novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein kinase (CaMK). J. Biol. Chem. 278, 18597–605.