PKA Kinase Enzyme System【子货号:V4246,包装:1 x 2,500 units,,运保温度:-70℃】
ADP-Glo™ Kinase Assay【子货号:V9101,包装:1 x 1,000 assays,,运保温度:-20℃】
描述:
Recombinant bovine cAMP-Dependent Protein Kinase (PKA), Catalytic Subunit, is expressed and purified from E. coli. Intracellular targets include ion channels (1), transcriptional activator proteins (2) and regulatory enzymes of glycogen metabolism (3). PKA does not require cAMP for activity, and the gene sequence can be found at accession number NM_174584.
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: PKA, 2,500 units (Bovine, recombinant full-length). MW: ~40kDa. Substrate: Kemptide (LRRASLG). Other: Reaction Buffer, DTT.
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
Bulk quantities available upon request.
References
1.Cohen, P. (1978) The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle. Curr. Top. Cell. Regul. 14, 117–96.
2.Rossie, S. and Catterall, W.A. (1987) Cyclic-AMP-dependent phosphorylation of voltage-sensitive sodium channels in primary cultures of rat brain neurons. J. Biol. Chem. 262, 12735–44.
3.Montminy, M.R. and Bilezikjian, L.M. (1987) Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene. Nature 328, 175–8.