Protein Kinase A, Type II Liquid. In 400 mM NaCl, 10 mM K2HPO4, 10 mM b-mercaptoethanol, 1 mM EDTA, pH 6.8. AVOID FREEZE/THAW CYCLES. Native PKA regulatory subunit type II purified from bovine heart. The molecular basis for regulation of cAMP-dependent protein kinase (PKA) resides in the ability of the dimeric regulatory subunit to bind to and inhibit two monomeric catalytic subunits in the absence of cAMP. The physical association of the catalytic subunit with the RII regulatory subunit purified from bovine heart blocks its catalytic activity in the cytoplasm and inhibits movement of catalytic subunit into the nucleus. Specific activity: ≥ 1000 units/µg protein. One unit is defined as the amount of enzyme required to inhibit incorporation of 1 pmol phosphate into Kemptide substrate by PKA catalytic subunit in 1 min at 30°C. Ref.: Corbin, J.D., et al. 1988. Methods Enzymol 159, 74. Rannels, S.R., et al 1983. Methods Enzymol 99, 55. Witt, J.J. and Roskoski, R. Jr. 1975. Anal Biochem. 66, 253. |
