Recombinant Human PKA C alpha Protein Summary
Description |
Recombinant protein for Human PKA C alpha Source:Baculovirus (Sf9 insect cells) Amino Acid Sequence:(NM_002730) |
Source |
Sf 9 (baculovirus) |
Protein/Peptide Type |
Recombinant Protein |
Gene |
PRKACA |
Purity |
>90%, by SDS-PAGE |
Applications/Dilutions
Dilutions |
|
Application Notes |
Specific activity: 137 nmol phosphate incorporated into Histone H1 per minute per mg protein at 30C for 15 minutes using a final concentration of 50 uM ATP (0.83 uCi/assay). |
Theoretical MW |
69 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -80C. Avoid freeze-thaw cycles. |
Buffer |
50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, 25% glycerol |
Concentration |
0.1 mg/ml |
Purity |
>90%, by SDS-PAGE |
Alternate Names for Recombinant Human PKA C alpha Protein
Background
Most of the effects of cAMP are mediated through the phosphorylation of target proteins on serine or threonine residues by the cAMP-dependent protein kinase (AMPK). The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. The mammalian catalytic subunit has been shown to consist of three PKA gene products: C-alpha, C-Beta , and C-gamma. Two PKA isoforms exist, designated types I and II, which differ in their dimeric regulatory subunits, designated RI and RII, respectively. Furthermore, there are at least four different regulatory subunits: RI-alpha, RI-Beta , RII-alpha, and RII-Beta . cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The catalytic subunit C-alpha of PKA (PKAca) is a member of the Ser/Thr protein kinase family and is a catalytic subunit C-Beta of AMPK. Tasken et al. assigned the PKAca gene to 19p13.1 (1). Yasuda et al found that protein kinase A is required for long-term potentiation in neonatal tissue and suggested that developmental changes in synapse morphology may underlie the changes in the kinase activity (2). Skalhegg et al generated a null mutation in the major catalytic subunit of PKAca, and observed early postnatal lethality in the majority of C-alpha knockout mice. Surprisingly, a small percentage of C-alpha knockout mice, although runted, survived to adulthood. In these animals, compensatory increases in C-Beta levels occurred in brain whereas many tissues, including skeletal muscle, heart, and sperm, contained less than 10% of the normal PKA activity (3).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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