Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Human PRKACB Antikörper:
anti-Rat (Rattus) PRKACB Antikörper:
anti-Mouse (Murine) PRKACB Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Human Polyclonal PRKACB Primary Antibody für ELISA, WB - ABIN545502
Higuchi, Yamashita, Yoshikawa, Tohyama: PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts. in The EMBO journal 2003
Show all 3 Pubmed References
Cbeta2 subunit of protein kinase A mRNA was up-regulated in prostate cancer and low expression of Cbeta2 mRNA in prostate cancer biopsies correlated with poor survival.
analysis of the mechanism underlying synergistic up-regulation of PDE4B2 via a cross-talk between PKA-Cbeta and p65
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.
activated by podophyllotoxin
PGE(2)-induced CYP1B1 expression is mediated by ligand-independent activation of the ERalpha pathway as a result of the activation of ERK, Akt, 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.
Data show that Phosphorylation of The(197) in the activation loop on protein kinase A decreased the K(m) by approximately 15- and 7-fold for kemptide and ATP, respectively.
Results suggest that PKA can negatively regulate ERalpha, at least in part, through FoxH1.
c-MYC 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 to promoter sequences.
Data describe the identification of a variant of the beta catalytic subunit of cyclic AMP-dependent protein kinase (PKACbeta) as a p75 neurotrophin receptor(NTR)-interacting protein, which phosphorylates p75(NTR) 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 and Cbeta.
there is a PKA-Cbeta-mediated inhibitory mechanism of p73 function
Murine lymphoid tissues express a protein that is a homologue of human protein kinase c subunit beta2
In conclusion, it seems that the Cbeta isoforms of PKA play different roles in proliferation and differentiation and could therefore be potential markers for prostate cancer progression.
Data provide the first evidence that Protein kinase C -beta play pivotal role in the regulation of AA production and cellular proliferation of human monocytoid MonoMac-6 cells.
Nuclear PKA C subunit co-locates with HA95 in splicing factor compartments and regulates pre-mRNA splicing, possibly through a cAMP-independent mechanism.
Recruitment of coactivator glucocorticoid receptor interacting protein 1 to an estrogen receptor transcription complex is regulated by the 3',5'-cyclic adenosine 5'-monophosphate-dependent protein kinase.
In human primary pigmented nodular adrenocortical disease tissues, dexamethasone paradoxically stimulates cortisol release through a glucocorticoid receptor-mediated effect on PKA catalytic subunits.
Findings show that PKIB and PKA-C kinase can have critical functions of aggressive phenotype of PCs through Akt phosphorylation and that they should be a promising molecular target for PC treatment.
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 kinase promoted by hydrogen peroxide in endothelial cells.
Protein kinase A signaling explains vasopressin-mediated regulation of membrane trafficking and gene transcription.
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 are dephosphorylated and activated in cilia and that impaired Gli2 and Gli3 processing in Ta3 mutant is at least in part due to a decrease in Gli2 and Gli3 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 (Cbeta) gene designated Cbeta5, Cbeta6 and Cbeta7.
These data suggest that both developmental and tumor phenotypes caused by Prkar1a mutation result from excess PKA activity due to PKA-Ca.
crystal structure of the catalytic subunit in complex with ADP, aluminum fluoride, Mg2+ ions and a substrate peptide was determined at 2.0 A resolution
glucose and glucagon-like polypeptide-1 caused translocation of Calpha 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
PKCbetaII is a target for colon cancer chemoprevention and the PKCbeta-selective inhibitor enzastaurin may represent an effective chemopreventive agent in patients at high risk for colon cancer.
Protein kinase A, C beta subunit 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.
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.
, cAMP-dependent protein kinase catalytic beta subunit isoform 4ab
, cAMP-dependent protein kinase catalytic subunit beta
, protein kinase A catalytic subunit beta
, p70 S6 kinase
, protein kinase, cAMP-dependent, catalytic, beta a
, C-beta subunit
, protein kinase, cAMP-dependent, catalytic, beta
, cAMP-dependent protein kinase C beta