|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for PRKACA(NM_002730.3) Search again
Product ID:
HQP014575
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CAFD1, PKACA, PPNAD4
Gene Description:
protein kinase cAMP-activated catalytic subunit alpha
Target Gene Accession:
NM_002730.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
|
|
| A | B |
|
Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
|
Summary
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. [provided by RefSeq].
Gene References into function
- Protein kinase A enhances, whereas glycogen synthase kinase-3 beta inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein D in a hierarchical fashion.
- regulation of the membrane binding of PKCalpha
- Katacalcin regulates human CD14+ PBMC migration via signaling events involving protein kinase A-dependent cAMP pathways.
- cAMP-induced inhibition of P-selectin expression is, in large part, mediated through activation of PKA.
- the effects of protein kinase A stimulation on sustained current in wild type and three disease-linked C-terminal mutant channels (D1790G, Y1795C, and Y1795H)
- Merlin was phosphorylated by PKA in cells in which PAK activity was suppressed, indicating that the two kinases function independently. PKA can phosphorylate merlin at serine 518, promoting heterodimerization between merlin and ezrin
- Inhibition of PKCalpha markedly inhibited IP3-induced activation of calcium the current.
- PKACA is involved in extracellular (Ca2+) signalling mediated by the calcium sensing receptor.
- repressor nuclear factor-kappaB p50/p50 binding to DNA depends on phosphorylation of Ser337 by the protein kinase A catalytic subunit
- Protein kinase A regulates caspase-9 activation by Apaf-1 downstream of cytochrome c
- a pseudopodial-located RhoA/ROCK/p38/NHE1 signal module is regulated by Protein Kinase A gating and then regulates invasion in breast cancer cell lines
- claudin-3 phosphorylation by PKA may provide a mechanism for the disruption of tight junctions in ovarian cancer
- A small but significant decrease in PKA, AKAP79, and PP2B in myometrial tissues from women in labor may contribute to a decrease in negative feedback on and enhancement of contractant signals at term
- Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion molecule glycoprotein regulates cell adhesion to laminin alpha5
- GCMa acetylation is mediated by CBP, which stimulates GCMa transcriptional activity through cyclic AMP/protein kinase A signaling
- CTP synthetase is phosphorylated by protein kinase A
- kinase inhibits the phosphatidylinositiol (3,4,5)-trisphosphate and Gbetagamma-mediated regulation of its activity
- Results imply a hindered transduction of the protein kinase A phosphorylation signal from cardiac troponin I to troponin C.
- analysis of a novel, noncanonical mechanism of modulation of beta-catenin signaling through direct phosphorylation of beta-catenin by PKA, promoting its interaction with CREB-binding protein
- These observations suggest that in primary pulmonary fibroblasts, PKCalpha but not PKCdelta or PKCepsilon mediate the profibrotic effect of CCL18.
- ATP binding specifically to the ATPC site in S2- InsP3R-1 controls the susceptibility of the receptor to protein kinase A-mediated phosphorylation
- Results suggest that gravin maintains a signaling complex that includes protein kinase A and phosphodiesterase 4D.
- transcriptomes associated with protein kinase A pathway was identified in human prostate cancer cells using Affymetrix GeneChip technology
- Thus, PAR2 activates PKCepsilon and PKA in sensory neurons, and thereby sensitizes TRPV1 to cause thermal hyperalgesia.
- analysis of a novel mechanism for the phosphorylation of MYPT3 by PKA and activation of the catalytic activity through direct interaction of a central region of MYPT3 with its N-terminal region
- Results suggest involvement of AMP-activated protein kinase in the control of expression of both metabolic genes, UCP3 and GLUT4, in the skeletal muscle of mice and of human newborns.
- STAT3 activation by G alpha(s) distinctively requires protein kinase A, JNK, and phosphatidylinositol 3-kinase
- Data show that activation-dependent expression of matrix metalloproteinases in peripheral blood mononuclear cells involves protein kinase A.
- activation of RankL gene expression by PKA- and gp130-inducers is mediated via common regulatory domains that also served to facilitate the activity of 1,25-(OH)2D3
- Rap1 mediates cyclic AMP-stimulated neurotensin secretion downstream of both Epac and protein kinase A signaling pathways
- Opposite roles for the protein kinase A transgene are defined in the formation of initial memories and extinction memories, representing the first genetic evidence that protein kinases may be constraints for the extinction of fear.
- LXRalpha is regulated not only by oxysterol derivatives but also by PKA-mediated phosphorylation, which suggests that nutritional regulation of SREBP-1c and lipogenesis could be regulated at least partially through modulation of LXR
- These results indicate that the reactive oxygen species-mediated TNF-alpha-induced IL-8 transcription is regulated by NF-kappaB/RelA phosphorylation at the critical Ser(276) residue by PKAc, resulting in stable enhanceosome formation on target genes.
- STAT-3 activation by DFMO is at least in part mediated through the PKA pathway
- PTH induces an increased activity of the eNOS system through PKA and PKC pathways
- Protein phosphorylation by PRKACA at Ser(637) results in clear alterations in Drp1 function and mitochondrial morphology.
- cyclic AMP-dependent protein kinase regulates proteasome function through phosphorylation of Rpt6
- The anx 2-S100A10/CFTR complex is important for CFTR function across epithelia.
- Nuclear PKA C subunit co-locates with HA95 in splicing factor compartments and regulates pre-mRNA splicing, possibly through a cAMP-independent mechanism.
- PKA and VEGFR2 converge at the MEK/ERK1/2 pathway to protect serum starved neuronal cells from a caspase-dependent cell death.
- PKA-dependent phosphorylation enhances the response of RyR2 to luminal Ca(2+) and reduces the threshold for SOICR and this effect of PKA is largely mediated by phosphorylation at Ser-2,030
- Contrary to the classical model of PKA activation, elevated cAMP does not allow RIalpha and Calpha to diffuse far apart unless the pseudosubstrate inhibitor PKI or locally concentrated substrate is coexpressed
- Prostaglandin E2 activates HPK1 kinase activity via a PKA-dependent pathway
- Protein kinase A, not Epac, suppresses hedgehog activity and regulates glucocorticoid sensitivity in acute lymphoblastic leukemia cells
- In patients with Alzheimer disease, over-activation of calpain because of calcium dysregulation causes increased degradation and thus decreased activity of PKA,which, in turn, contributes to down-regulation of CREB and impaired cognition and memory.
- Vitamin K(2) modulates its target gene expression in osteoblastic cells through the PKA-dependent mechanism.
- This study demonstrates that the phosphorylation of p50 and p65 by the catalytic subunit of protein kinase A (PKAc) is essential for NF-kappaB DNA binding and transactivation activity.
- Data suggest that PKA effects on IFNT regulation might be mediated through CBP/p300 coactivation, particularly as CBP and Ets2 occupy the proximal promoter region of IFNT in bovine trophoblast CT-1 cells.
- These results suggest a novel mechanism of ANP protective effects against agonist-induced pulmonary endothelial cell barrier dysfunction via inhibition of Rho signaling by Epac/Rap1-Rac and PKA signaling cascades.
- analysis of allosteric cooperativity in protein kinase A
- The results herein provide initial evidence that the inhibitory effect of hypoxia on MMP-9 by mature dendritic cells requires the activation of A(2b) in a cAMP/PKA-dependent pathway.
- Data provide the first evidence that 17beta-estradiol can inhibit PKA overactivation and PKA-induced tau hyperphosphorylation, implying a preventive role of 17beta-estradiol in AD-like tau pathology.
- The selective use of PKA and Epac-1 pathways to inhibit distinct aspects of fibroblast activation illustrate the pleiotropic ability of PGE(2) to inhibit diverse fibroblast functions.
- A switch to type II PKA activity is not necessary for increased kinase activity or tumorigenesis.
- Androgen actively evokes a nongenomic signaling pathway to activate PKA that is needed for the genomic functioning of nuclear androgen receptor.
- activation of protein kinase A elicits an immediate response through induction of genes such as ID2 and FosB, followed by sustained secretion of bone-related cytokines such as BMP-2, IGF-1, and IL-11
- growth factor signals promote phosphorylation of ER coactivator PELP1 via PKA pathway, and such modification may have functional implications in breast tumors with deregulated growth factor signaling
- The distribution of DNA-PK between nuclear and cytoplasmic compartments can thus potentially be influenced by relative inputs of cAMP signaling through the EPAC and PKA pathways.
- HPV16 E7-dependent transformation activates NHE1 through a PKA-RhoA-induced inhibition of p38alpha.
- PKA activates human HSL against lipid substrates in vitro primarily through phosphorylation of Ser649 and Ser650