cAMP-dependent Protein Kinase (PKA), catalytic subunit
The catalytic subunit of cAMP-dependent Protein Kinase (PKA) is a serine/threonine protein kinase. The recognition motif for phosphorylation by PKA is RRXS/TY, where Y tends to be a hydrophobic residue.
- Recombinant enzyme with no detectable protease or phosphatase contaminating activities
- Optimal activity and stability for up to 12 months
The catalytic subunit of cAMP-dependent Protein Kinase (PKA) is a serine/threonine protein kinase, which combines, in the absence of cAMP, with the regulatory subunit to form the inactive PKA holoenzyme. Since this is the free catalytic subunit alone, no cAMP is required for activation (1,2).
When purified from mammalian tissue, the PKA catalytic subunit is always phosphorylated at T197, essential for catalysis. Most likely a heterologous kinase is responsible for this in vivo phosphorylation of PKA. Although the fully active PKA expressed in E. coli autophosphorylates on both T197 and S338, this does not reflect the mechanism used in eukaryotic cells (3).
Product SourceIsolated from a strain of E. coli that carries a clone expressing the murine PKA catalytic subunit (α isoform) under control of a T7 expression system (2,3) (cDNA kindly provided by Dr. G.S. McKnight).
Recognition DeterminantThe recognition motif for phosphorylation by PKA is RRXS/TY, where Y tends to be a hydrophobic residue. A Phe in the nearby sequence tends to be a negative determinant for phosphorylation by PKA. Some variations with regard to spacing and basic residues are permissible (2,4).
The following reagents are supplied with this product:
Store at (°C) Concentration NEBuffer™ for Protein Kinases (PK) -20 10X
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