The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
A kinase (PRKA) anchor protein 10
A kinase anchor protein 10
A kinase anchor protein 10 mitochondrial
A-kinase anchor protein 10
D AKAP 2
Dual specific A kinase anchoring protein 2
Dual specificity A kinase-anchoring protein 2
Mitochondrial A kinase PPKA anchor protein 10
Protein A kinase anchoring protein 10
Protein A kinase anchoring protein 10 mitochondrial precursor
Protein kinase A anchoring protein 10
Protein kinase A-anchoring protein 10
Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase.
Genetic variations in AKAP10 are a cause of susceptibility to sudden cardiac death (SCD) [MIM:115080]. Unexpected rapid natural death due to cardiovascular collapse within one hour of initial symptoms. It is usually caused by the worsening of existing heart diseases. The sudden onset of symptoms, such as chest pain and cardiac arrhythmias, particularly ventricular tachycardia, can lead to the loss of consciousness and cardiac arrest followed by biological death. Note=Increased susceptibility to sudden cardiac death may be conferred by AKAP10 variants that are associated with markers of low vagus nerve sensitivity, e.g. fast basal heart rate and low heart rate variability.
Contains 2 RGS domains.
RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.
Mitochondrion. Membrane. Cytoplasm. Predominantly mitochondrial but also membrane associated and cytoplasmic.