Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human PRKACA Protein expressed in Wheat germ - ABIN1316219
Loilome, Yooyuen, Namwat, Sithithaworn, Puapairoj, Kano, Noguchi, Miwa, Yongvanit: PRKAR1A overexpression is associated with increased ECPKA autoantibody in liver fluke-associated cholangiocarcinoma: application for assessment of the risk group. in Tumour biology 2012
PRKACA mutations are highly specific for cortisol over-secretion, while they are absent or very rare in the context of other adrenal diseases. Patients carrying these somatic mutations are affected by a more severe phenotype and are identified at a younger age.
Somatic mutations in PRKACA, coding for the catalytic alpha subunit (show POLG Proteins) of protein kinase A (PKA), have been recently identified as the most frequent genetic alteration in cortisol-secreting adrenocortical adenomas, which are responsible for adrenal Cushing's syndrome.
HIF1a (show HIF1A Proteins) transcriptional activity is stimulated by Protein kinase A-dependent phosphorylation
cigarette smoke extracts activate the PKA, CREB (show CREB1 Proteins), and IL-13Ralpha2 axis in lung endothelial cells.
Data indicate a subpopulation of the CaV1.2 (show CACNA1C Proteins) channel pore-forming subunit (alpha1C) within nanometer proximity of protein kinase A (PKA) at the sarcolemma of murine and human arterial myocytes.
we propose that the PKA-Smurf1 (show SMURF1 Proteins)-PIPKIgamma pathway has an important role in pulmonary tumorigenesis and imposes substantial clinical impact on development of novel diagnostic markers and therapeutic targets for lung cancer treatment.
The mutated PRKACA proteins lost their ability to bind to PRKAR1A (show PRKAR1A Proteins), and thereby lead to constitutive activation of the PKA pathway. Together with previous reports of PRKAR1A (show PRKAR1A Proteins) mutations in syndromic cardiac myxoma, our study demonstrates the importance of the PKA pathway in the tumourigenesis of cardiac myxoma.
differential regulation of PKA and cell stiffness in unconfined versus confined cells is abrogated by dual, but not individual, inhibition of Piezo1 and myosin II.
PRKACA mutations are present in cortisol-producing adenomas and bilateral adrenal macronodular hyperplasia. PRKACA mutation is associated with more severe autonomous cortisol secretion.
Dual co-expression of human fetal Tau with PKA in Escherichia coli results in multisite Tau phosphorylation including also naturally occurring sites which were not previously considered in the context of 14-3-3 (show YWHAQ Proteins) binding. Tau protein co-expressed with PKA displays tight functional interaction with 14-3-3 (show YWHAQ Proteins) isoforms of a different type.
PKA and MEK (thus, also pERK) are the intracellular mediators downstream of GPR30 that induce the non-genomic suppression of GnRH-induced LH secretion from bovine AP cells by estradiol or G1
Data indicate that mitochondrial cAMP-dependent protein kinase (PKA) activity is regulated by the protease calpain.
structural basis of selectivity for protein kinase A in complex with Rho-kinase (show ROCK1 Proteins) inhibitors by x-ray crystallography
Purification and characterisation of protein kinase catalytic subunit (PKAcat) from bovine lens.
ceramide as a potent physiological modulator of the Na(+)-ATPase, participating in a regulatory network in kidney cells and counteracting the stimulatory effect of PKA via PKCzeta (show PRKCZ Proteins)
we demonstrate that PKA, PKC (show FYN Proteins) and PI3K pathways crosstalk in porcine male germ cells to crucially regulate GSK3A (show GSK3a Proteins) phosphorylation which subsequently controls cell motility.
Generation of the Dnajb1 (show DNAJB1 Proteins)-Prkaca fusion gene in wild-type mice to be sufficient to initiate formation of tumors that have many features of human fibrolamellar hepatocellular carcinonma.
S1928A KI mice failed to induce long-term potentiation in response to prolonged theta-tetanus (PTT-LTP (show SCP2 Proteins)), a form of synaptic plasticity that requires Cav1.2 (show CACNA1C Proteins) and enhancement of its activity by the beta2-adrenergic receptor (show ADRB2 Proteins) (beta2AR (show ADRB2 Proteins))-cAMP-PKA cascade.
Data show that laminin alpha2beta1gamma1 (Lm211) can inhibit neuregulin 1 (show NRG1 Proteins) type III (Nrg1III) by limiting protein kinase A (PKA) activation, which is required to initiate myelination.
study identifies a new role of Dual-AKAP1 (show AKAP1 Proteins) in regulating mitochondrial trafficking through Miro-2 (show RHOT2 Proteins), and supports a model in which PINK1 (show PINK1 Proteins) and mitochondrial PKA participate in a similar neuroprotective signaling pathway to maintain dendrite connectivity
Data suggest that enzyme activation by cAMP involves highly stable conformation of Prkar1a as it binds to Prkaca; glycine residue, G235, appears to function as hinge in B/C helix conserved in Prkar1a; this "Flipback" conformation plays role in cAMP association to A domain of Prkar1a. (Prkar1a = cyclic AMP-dependent protein kinase RIalpha subunit; Prkaca = cyclic AMP-dependent protein kinase catalytic subunit)
cAMP dependent protein kinase A (PKA) is a key intracellular factor mediating SHH (show SHH Proteins) signaling through regulation of GLI3 (show GLI3 Proteins) processing.
this study shows illustrates for the first time the ability of protein kinase A to increase colony-stimulating factor 1 receptor (show CSF1R Proteins) DNA methylation (show HELLS Proteins) resulting in macrophage maturation
these results suggest that the activation of 5-HT1D receptors selectively enhanced IA via the Gbetagamma of the Go-protein, PKA, and the sequential B-Raf (show SNRPE Proteins)-dependent p38 MAPK (show MAPK14 Proteins) signaling cascade.
support hypothesis that PRKACA activation is responsible for downstream protein tyrosine phosphorylation events in stallion sperm
Thus Ca(2 (show CA2 Proteins)+)-cAMP/PKA-dependent phosphorylation limits the rate and magnitude of increase in spontaneous action potential firing rate.
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. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
, cAMP-dependent protein kinase catalytic subunit alpha
, protein kinase A catalytic subunit
, cAMP-dependent protein kinase catalytic subunit C alpha
, protein kinase A
, protein kinase, cAMP-dependent, catalytic, alpha
, C-alpha subunit
, sperm cAMP-dependent protein kinase catalytic subunit
, protein kinase A alpha
, PKA catalytic subunit alpha