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Human Polyclonal PRKAR2A Primary Antibody pour WB - ABIN519185
Uys, Ramburan, Loos, Kinnear, Korkie, Mouton, Riedemann, Moolman-Smook: Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C. dans BMC cell biology 2011
High PK-R2 expression is associated with colorectal cancer.
Prkar2a deficiency predisposes to hematopoietic malignancies in vivo. RIIalpha's likely association with HS and DLBCL was hitherto unrecognized and may lead to better understanding of these rare neoplasms.
Disruption of Snapin-PKR2 interaction did not affect PKR2 signaling, but increased the ligand-induced degradation, implying a role of Snapin in the trafficking of PKR2.
we demonstrate that neurochondrin has strong isoform selectivity towards the RIIa subunit of PKA with nanomolar affinity
Results show that mouse Prkar1a and human PRKAR2A exhibited a dynamic spatio-temporal expression in tooth development, whereas neither human PRKAR1A nor mouse Prkar2a showed their expression in odontogenesis.
These data demonstrate that some Kallmann syndrome-associated, intracellularly retained mutant PKR2 receptors can be functionally rescued, suggesting a potential treatment strategy for patients bearing such mutations.
while there is no change in type II regulatory (RIIalpha) or catalytic (Calpha) subunit expression, site specific RIIalpha (Ser96) and Calpha (Thr197) phosphorylation are increased in heart failure, as well as expression of type I regulatory subunit (RI)
Smad4 and the R subunit of the protein kinase A holoenzyme form a functional complex in vivo in response to TGFbeta.
RIaalpha and RIIaalpha were identified as cCMP-binding proteins.
ETO nervy homology region (NHR) 3 domain-PKA(RIIalpha) protein interaction does not appear to significantly contribute to AML1-ETO's ability to induce leukemia.
findings indicate that increased particulate type II protein kinase A activity occurs throughout pregnancy therefore directing the cAMP quiescence signal to specific subcellular loci within myometrial smooth muscle cells
switching of PKA isozyme can cause tumor cells to undergo phenotypic reversion of the malignancy [revoew]
These data implicate the involvement of PKA-RIIalpha anchoring apical targeting of distinct proteins and glycosphingolipids to apical plasma membrane domains and suggest that rerouting may underlie the delayed Golgi-to-apical surface transport of MDR1.
The high-resolution crystal structures of the docking and dimerization (D/D) domain of the RIIalpha regulatory subunit of PKA in complex with the high-affinity anchoring peptide AKAP-IS explain the molecular basis for AKAP-regulatory subunit recognition.
The data suggest that centrosomal anchoring of RIIalpha and the interrelated subapical positioning of these centrosomes is required for oncostatin M-, but not cAMP-mediated, bile canalicular lumen development.
RIIalpha releases Calpha upon elevated cAMP alone, dependent on autophosphorylation of the RIIalpha inhibitory domain
Bacillus anthracis edema toxin altered the protein levels and activity of protein kinase A and exchange protein activated by cAMP (Epac), a recently identified cAMP-binding molecule.
Analyses of the involvement of PKA regulation mechanism in meiotic incompetence of porcine growing oocytes.
angle X-ray scattering studies indicate RIalpha, RIIalpha, and RIIbeta homodimers differ markedly in overall shape despite extensive sequence homology and similar molecular masses;cAMP binding does not cause large conformational changes(Prkar1a, Prkar2a)
RII phosphorylation precedes cAMP binding and controls the inactivation by modulating the reassociation involving the coordinated action of phosphodiesterases and phosphatases.
PGD2-DP1 axis-induced M2 polarization facilitates resolution of inflammation through the PRKAR2A-mediated suppression of JAK2/STAT1 signaling.
Disruption of the ubiquitously expressed PKA RIIalpha subunit in mice confers resistance to diet-induced obesity, glucose intolerance, and hepatic steatosis.
Results indicte that Cypher/ZASP interacted with the regulatory subunit RIIalpha of PKA.
a key role for AKAP-targeted PKA in control of heart rate and contractile function
protein kinase A type II is activated by sphingosine through a novel cAMP-independent mechanism
The RII alpha regulatory subunit of protein kinase A is not required for normal T cell development, homeostasis, and the generation of a cell-mediated immune response in vivo.
crystal structure of RIIalpha holoenzyme solved and compared to the RIalpha holoenzyme; structure demonstrates the conserved and isoform-specific features of RI and RII and the importance of ATP
AKAP121 and PKAR2A serve to enhance steroidogenesis by directing the synthesis and activation of STAR at the mitochondria in response to cAMP.
protein kinase cAMP dependent regulatory type II alpha showed a clear-cut double striation pattern on each m-line and z-line.
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 one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of cAMP-dependent protein kinase. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER).
cAMP-dependent protein kinase regulatory subunit RII alpha
, cAMP-dependent protein kinase type II-alpha regulatory subunit
, protein kinase A, RII-alpha subunit
, cAMP-dependent protein kinase, regulatory subunit alpha 2
, protein kinase, cAMP-dependent, regulatory, type II, alpha
, cAMP-dependent protein kinase type II-alpha regulatory subunit-like
, protein kinase cAMP-dependent regulatory type II alpha
, protein kinase, cAMP-dependent, regulatory, type 2, alpha
, LOW QUALITY PROTEIN: cAMP-dependent protein kinase type II-alpha regulatory subunit