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Synonyms
PKA, cAMP-dependent protein kinase catalytic subunit alpha
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Alternative_names
PKA, cAMP-dependent protein kinase catalytic subunit alpha
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Description
Involved in regulation of glycogen, sugar, and lipid metabolism
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Recombinant
Yes
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Source
Baculovirus (Sf9 insect cells)
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Purity by SDS PAGE
≥90%
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Assay
SDS-PAGE
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Activity Specifications test method
342 µmol phosphate incorporated into CREBtide substrate per minute per mg protein at 30°C for 15 minutes using a final concentration of 50 µM ATP (0.83 µCi/assay).
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Molecular Weight
65.0 kDa
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Storage Temp
-80°C
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Shipping
dry ice
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Shelf Life
12 months
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Concentration
5µg/50 µl
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Appearance
Liquid
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Physical form description
Recombinant proteins in storage 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).
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Background Information
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 (PKA). 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-α, C-β, and C-γ. 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-α, RI-β, RII-α, and RII-β. The 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-β of PKA (PKAcb) is a member of the Ser/Thr protein kinase family and is a catalytic subunit C-β of AMPK. Berube et al. assigned the PKAcb to human chromosome 1 by Southern blot analysis of somatic cell hybrids (1) and Simard et al located it to 1p36.1 by in situ hybridization (2).
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Handling
Centrifuge the vial prior to opening.
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Usage
For Research Use Only! Not to be used in humans
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