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We suggest a role of the PRKACB gene splice variant Cbeta2 in regulating innate as well as adaptive immune sensitivity in vivo.
Gli2 and Gli3 (show GLI3 Proteins) are dephosphorylated and activated in cilia and that impaired Gli2 and Gli3 (show GLI3 Proteins) processing in Ta3 (show HSP90B1 Proteins) mutant is at least in part due to a decrease in Gli2 and Gli3 (show GLI3 Proteins) phosphorylation.
Data indicate that TRPV4 activity and TRPV4 trafficking are under discrete but synergistic control of PKC- and PKA-dependent pathways.
Studies identified three novel alternatively spliced transcript variants of the mouse protein kinase A catalytic beta subunit (show POLG Proteins) (Cbeta) gene designated Cbeta5, Cbeta6 and Cbeta7.
These data suggest that both developmental and tumor phenotypes caused by Prkar1a (show PRKAR1A Proteins) mutation result from excess PKA activity due to PKA-Ca.
crystal structure of the catalytic subunit in complex with ADP, aluminum fluoride, Mg2 (show MCOLN1 Proteins)+ ions and a substrate peptide was determined at 2.0 A resolution
glucose and glucagon (show GCG Proteins)-like polypeptide-1 caused translocation of Calpha (show PRKACA Proteins) to the nucleus and of Cbeta to the plasma membrane and the nucleus, but did not affect the distribution of Cgamma in pancreatic beta-cells
Murine lymphoid tissues express a protein that is a homologue of human and bovine Cbeta2
Protein kinase A, C beta subunit (show POLG Proteins) is not essential for neuronal development or function but may play a more subtle role in memory that is modulated by strain-specific genetic modifiers.
analysis of the mechanism underlying synergistic up-regulation of PDE4B2 via a cross-talk between PKA-Cbeta and p65 (show GORASP1 Proteins)
The gene polymorphism loci rs12132032 in PRKACB maybe a potential risk factor for anencephaly in Chinese population from Shanxi, while gender susceptibility may influence the correlation.
The previously unknown small molecule inhibitor-dependent interaction of Cbeta1 with the cell cycle and apoptosis regulatory protein-1 was verified.
PGE (show LIPF Proteins)(2)-induced CYP1B1 (show CYP1B1 Proteins) expression is mediated by ligand-independent activation of the ERalpha (show ESR1 Proteins) pathway as a result of the activation of ERK (show EPHB2 Proteins), Akt (show AKT1 Proteins), and PKA in breast cancer cells.
Data show that PI3K activation and PIP3 production lead to recruitment of the PKB/beta-arrestin/PDE4 complex to the membrane via the PKB PH domain, resulting in degradation of the TCR-induced cAMP pool and allowing full T-cell activation to proceed.
Results suggest that PKA can negatively regulate ERalpha (show ESR1 Proteins), at least in part, through FoxH1 (show FOXH1 Proteins).
c-MYC (show MYC Proteins) induces the activity of protein kinase A by inducing the transcription of the gene encoding the PKA catalytic subunit beta in multiple tissues, independent of cell proliferation by direct binding of c-MYC (show MYC Proteins) to promoter sequences.
Data describe the identification of a variant of the beta catalytic subunit of cyclic AMP (show APRT Proteins)-dependent protein kinase (show CDK7 Proteins) (PKACbeta) as a p75 neurotrophin receptor (show NGFR Proteins)(NTR)-interacting protein, which phosphorylates p75(NTR (show NGFR Proteins)) at Ser304.
there are abnormalities in [3H]cAMP binding and catalytic activity kinase A in brain of depressed suicide victims, which could be due to reduced expression of RIIbeta (show PRKAR2B Proteins) and Cbeta.
there is a PKA-Cbeta-mediated inhibitory mechanism of p73 (show TP73 Proteins) function
Murine lymphoid tissues express a protein that is a homolog of bovine Cbeta2 (protein kinase c subunit beta2).
critically involved in mediating the phosphorylation of AMP (show TMPRSS5 Proteins) kinase promoted by hydrogen peroxide in endothelial cells.
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Several alternatively spliced transcript variants encoding distinct isoforms have been observed.
p70 S6 kinase
, protein kinase, cAMP-dependent, catalytic, beta a
, protein kinase, cAMP-dependent, catalytic, beta
, cAMP-dependent protein kinase catalytic subunit beta
, PKA C-beta
, cAMP-dependent protein kinase C beta
, cAMP-dependent protein kinase catalytic beta subunit isoform 4ab
, protein kinase A catalytic subunit beta
, C-beta subunit