GeneTex
United States (US)

PKA C alpha (Active) recombinant protein

Cat No. GTX65206

Application ELISA, Functional Assay, Apuri, Blocking
Reactivity Human
Species Human
APPLICATION

Application Note

137 nmol phosphate incorporated into Histone H1 per minute per mg protein at 30ºC for 15 minutes using a final concentration of 50 uM ATP (0.83 uCi/assay).

Calculated MW

69.0 kDa. ( Note )
PROPERTIES

Form

Liquid

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

Storage

Store at -80ºC. Product is stable for at least 6-12 months.

Concentration

0.1mg/ml(Please refer to the vial label for the specific concentration.)

Antigen Species

Human

Expression System

Baculovirus (Sf9 insect cells)

Purification


Purity was assessed by SDS-PAGE (≥90%) and by HPLC.

Note

For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
TARGET

Synonyms

Protein Kinase Camp-Activated Catalytic Subunit Alpha,Pkaca,Ppnad4,Prkaca

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).

Research Area

Package List Price ($)
$ 359