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Validated All-in-One™ qPCR Primer for PRKCA(NM_002737.2) Search again
Product ID:
HQP014706
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AAG6, PKC-alpha, PKCA, PKCI+/-, PKCalpha, PRKACA
Gene Description:
protein kinase C alpha
Target Gene Accession:
NM_002737.2(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:
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| A | B |
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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. |
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Summary
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been reported to play roles in many different cellular processes, such as cell adhesion, cell transformation, cell cycle checkpoint, and cell volume control. Knockout studies in mice suggest that this kinase may be a fundamental regulator of cardiac contractility and Ca(2+) handling in myocytes. [provided by RefSeq].
Gene References into function
- activation required for vitamin C-succinate induced apoptosis of HL-60 cells
- Four residues located near the calcium binding site of PKC alpha are critical for activation and in vivo membrane translocation of the enzyme.
- Isoforms of protein kinase C and their distribution in human adrenal cortex and tumors
- PKCalpha is required for ET-1-induced human myometrial cell growth
- the first report of focal adhesion kinase and phosphatidylinositol 3-kinase-dependent PKC-alpha activation in bacterial invasion related to cytoskeletal reorganization
- role in induction of metallproteinases 1 and 3 in fibroblasts by basic calcium phosphate crystals
- Calcium-dependent involucrin expression is inversely regulated by protein kinase C (PKC)alpha and PKCdelta.
- PKC alpha expressed in human neutrophils can phosphorylate p47phox and induce both its translocation and NADPH oxidase activation as well as the binding of p47phox to the cytosolic fragment of p22phox.
- Data show that protein kinase Calpha mediates the effect of antiarrhythmic peptide on gap junction conductance.
- REVIEW:Interaction of protein kinase C isozymes with membranes containing anionic phospholipids utilizing fluorescent phorbol esters to probe the properties of the C1 domains
- PKC alpha functions as a negative modulator of calcineurin-regulated retinoid X receptor responsive element-dependent transcription during T cell activation.
- A294G mutation of protein kinase C alpha does not detectably affect its biochemical properties in vitro or in vivo, and is at least rare in thyroid neoplasias
- Cis activation of the basal promoter of the PKC alpha gene occurs through an activator protein-2-dependent, phorbol ester-responsive pathway, which suggests an autoregulatory manner of transcription in glioblastoma multiforme cells.
- Alpha-tocopherol decreases superoxide anion release in human monocytes under hyperglycemic conditions via inhibition of protein kinase C-alpha.
- Protein kinase C alpha plays an important role in activating store-operated Ca2+ channels (SOC) in human mesangial cells
- Activation of PKCalpha stabilizes F-actin and thereby opposes the effect of PKCepsilon on membrane remodeling in T84 cells.
- Our findings present original data that PKCalpha is the isoform specifically involved in the proliferation of primary human osteoblasts.
- greater increase of PKCalpha translocation after PMA treatment in breast cancer erythrocytes compared to controls was observed
- Il-2 increased protein kinase C alpha expression, but polysaccharide K decreased it.
- the direct PKC-dependent activation of the amyloid protein precursor secretory pathway is compromised by reduced PKCalpha expression and a specific role of this isoform in these mechanisms
- PKCalpha may regulate Ets1 activity in invasive breast cancer cells
- PKC alpha plays a necessary role in mediating calcium-induced differentiation. Failure to regulate PKC alpha in SCC4 carcinoma cells may underlie at least part of the failure of calcium to promote differentiation in these cells.
- Filamin A was identified as a direct binding partner of protein kinase Calpha; two binding sites were identified on filamin A; a Ca2+ and phospholipid-dependent association of the regulatory domain of protein kinase C with these sites was revealed.
- PKCalpha is involved in the regulation of Ca2+-induced platelet aggregation.
- data demonstrate a pathway of Rho activation involving protein kinase c alpha-dependent phosphorylation of p115Rho guanine exchange factor
- The novel varepsilon and eta and atypical zeta, but not the conventional alpha and beta and the novel delta PKCs, may be involved in the signaling pathways involved in thrombin-induced human platelet P-selectin expression
- Protein kinase C promotes apoptosis in LNCaP prostate cancer cells through activation of p38 MAPK and inhibition of the Akt survival pathway
- protein kinase C alpha associates with phospholipase D1 and enhances basal phospholipase D activity in a protein phosphorylation-independent manner in melanoma cells, which contributes to the cell's high invasive potential.
- Protein kinase C alpha negatively regulates cell spreading and motility in breast cancer cells.
- PKC alpha phosphorylates diacylglycerol kinase zeta in cells, and this phosphorylation inhibits its kinase activity to remove cellular diacylglycerol, thereby affecting cell growth.
- Loss of protein kinase Calpha expression may enhance the tumorigenic potential of Gli1 in basal cell carcinoma.
- protein kinase C alpha signaling is activated by apolipoprotein A-I, and it has a role in phosphorylation and stabilization of ATP binding cassette transporter A1 for the high density lipoprotein assembly
- the affinity of isolated C1A and C1B domains of PKCalpha and PKCgamma for soluble and membrane-incorporated DAG and phorbol ester were measured by isothermal calorimetry and surface plasmon resonance in order to compare activation mechanisms
- there is an impairment of degradation of protein kinase c alpha in huntington disease 150q cells that is connected with the sequestration of proteasome on mutant huntingtin aggregates
- PKCA acts upstream of PKCtheta to activate IkappaB kinase and NF-kappaB in T-lymphocytes.
- PKCalpha and betaII have roles in the regulation of membrane recycling
- in gastric cancer, protein translocation of PLCgamma2 and PKCalpha is critical event in the process of apoptosis induction.
- PKC-alpha and PKC-epsilon act cooperatively in regulating JNK activation in response to PMA
- Only PKC-alpha is involved in the signal transduction cascade leading to neutrophil transepithelial migration.
- PKC alpha is a critical regulatory element that is required for efficient regulatory volume decrease in HeLa cells
- PKCalpha-S100C/A11-mediated pathway is involved in and essential for the growth inhibition of normal human keratinocytes cells by TGFbeta1.
- PKD activation plays a central role in NT peptide secretion; upstream regulators of PKD include PKC-alpha and -delta and Rho/ROK
- There was expression of protein kinase C alpha in abnormal muscle fibers. Protein kinase C isoforms may play a role in the pathogenesis of myofibrillar myopathy.
- PKCA has a major role in cytoskeleton-dependent avidity modulation of ALCAM.
- protein kinase C alpha, iota, and theta binding to L-selectin cytoplasmic domain is modulated by receptor phosphorylation
- Results suggest that the involvement of protein kinase C alpha in carbachol-induced soluble amyloid precursor protein (sAPPalpha) release is negligible, but PKC epsilon may be important in coupling cholinergic receptors with APP metabolism.
- phosphorylation of LRP by PKCalpha modulates the endocytic and signaling function of LRP by modifying its association with adaptor proteins
- autophosphorylation of PKCalpha limits its sensitivity to DAG; kinase inhibitors augment the DAG sensitivity of PKCalpha by destabilizing the closed conformation
- Use of PKC agonists and isozyme-specific pseudosubstrate peptide antagonists suggested a role for PKCalpha and -epsilon in VEGF-mediated DAF up-regulation, mediating A cytoprotective pathway in ECs.
- Results propose a new mechanism by which lithium indirectly inhibits glycogen synthase kinase-3beta via phosphatidylinositol 3 kinase-dependent activation of protein kinase C alpha.
- We analyzed the dependence of the expression of some selected protein kinase C isoenzymes on the availability and/or action of androgens.
- PKC-alpha-mediated NG2 phosphorylation at Thr(2256) is a key step for initiating cell polarization and motility
- central role of PKC isoforms and the negative regulatory function of c-Src in the control of stromelysin 3 expression
- Ets1 serves as an effector for PKCalpha to fulfil certain functions in cancer ce
- we used publicly available gene expression array data to further understand PKC-a-associated gene expression profiles in NSCLC
- protein kinase Calpha transcriptional repression via Sp1 by wild type p53 is involved in inhibition of multidrug resistance 1 P-glycoprotein phosphorylation
- colocalizes with virus particles and is required for Respiratory syncytial virus (RSV) fusion to the cell membrane of bronchial epithelial cells
- diacylglycerol-responsive PKC isoforms differentially influence CaR agonist-induced release of Ca2+ from internal stores
- Calpha activation and phosphorylation of syntaxin 4 and Munc18c are required for the cell surface expression of P-selectin and the consequent binding of neutrophils to endothelial cells.
- there is a complex interplay between PKCalpha, Syk, and Src involving physical interaction, phosphorylation, translocation within the cell, and functional activity regulation
- protein kinase C has a role in chitosan glutamate-mediated tight junction disruption
- Epidermal and hepatocyte growth factors, but not keratinocyte growth factor, modulate protein kinase Calpha translocation to the plasma membrane
- two fatty acids inhibited the phorbol 12-myristate 13-acetate (PMA)-induced plasma membrane translocation of protein kinase C (PKC)-alpha and -epsilon
- Results demonstrate that a branched signaling pathway involving MEK, ERK, PKCepsilon, PKCalpha, and caveolin-1 regulates collagen expression in normal lung tissue and is perturbed during fibrosis.
- NAG-1 expression is up-regulated by TPA in LNCaP cells through a PKC-dependent pathway involving the activation of NF-kappa B
- Inhibition of the oxidative burst, i.e., cellular desensitization, was clearly reversed in cells overexpressing PKC alpha, pointing to PKC alpha as the major transmitter in eliciting the oxidative burst in monocytes/macrophages.
- PKCalpha is specifically required for TPA-induced ERK(MAPK) signaling to trigger gene expressions of p15(INK4b) and p16(INK4a) leading to HepG2 growth inhibition
- PRKCA-dependent PRKD1 activation modulates ERK signal pathway and endothelial cell proliferation by vascular endothelial growth factor A.
- PKCalpha C1A-C2 interdomain interactions have a role in lipid-mediated PKCalpha activation
- The data do not support a strong association between single nucleotide polymorphism of PRKCA and spina bifida risk.
- PKCalpha stimulates NO production in endothelial cells and plays a role in regulation of blood flow in vivo.
- Results identify targets in RLIP76 for phosphorylation by protein kinase C alpha, which may act as substrates for differential transport of doxorubicin.
- PKC stimulation upregulates neuron-specific ELAV (nELAV) proteins (HuB, HuC, and HuD), and induces nELAV proteins to colocalize with the translocated PKCalpha isozyme on the cytoskeleton, with a concomitant increase of nELAV threonine phosphorylation.
- Ca2+-activated PKCalpha and its isolated C2 domain localize exclusively to the plasma membrane
- PKCalpha expression may be modulated by Elk-1 and MZF-1 at the transcriptional level.
- Thrombin is able to induce activation of caspases 3 and 9 in human platelets and significantly increases the amount in the cytoskeleton of the active forms of both caspases and the procaspases 3 and 9.
- protein phosphorylation and dephosphorylation via PKC and the corresponding protein phosphatases contribute to phosphatidylserine exposure and erythrocyte shrinkage after energy depletion
- increased expression of PKC-alpha and -betaI leads to increased total classical PKC kinase activity; increased activity of the isoenzymes plays a role in accelerated growth of TCC. In carcinoma tissue, PKC expression and activity are under strict control
- Data show that protein kinase C-alpha activation in endothelial cells leads to upregulation of sphingosine kinase-1 expression and activity, which is critically involved in the mechanism of endothelial cell migration.
- Inhibition of Protein Kinase C represents a mechanism by which high tyrosine kinase activity can enhance cellular Ca(2+) transients and thus exert profound effects on the proliferation, apoptosis and chemotaxis of leukemic cells.
- PKC alpha mmodulates Bcl2 phosphorylation and is relevant to chemoresistance in acute myeloid leukemia
- effect of insulin is dependent on activation of PKCalpha and/or PKCbeta, and these insulin signals may interfere with the dynamic assembly/disassembly and/or distribution of F-actin, which is required for the phagocytosis process
- PKCalpha activation is a critical step in androgen receptor nuclear exclusion by melatonin.
- In conclusion, although CDCA and UDCA activate different PKC isoforms, PKCalpha plays a major role in the bile acid-induced inhibition of cAMP synthesis in fibroblasts.
- PKC regulates sequestration of recycling molecules into this compartment, the pericentrion; PKC acted distal to the site of internalization of endocytic cargo
- Incubation of podocytes with membranous glomerulonephritis sera determined strong upregulation of pPKC-alpha/beta that was reverted by pre-incubation with clusterin
- RLIP76-/- mouse embryonic fibroblasts were resistant to PKCalpha-depletion mediated growth inhibition, as well as to the PKCalpha-dependent mitogen, phorbol 12-myristate 13-acetate (PMA).
- WISP-2/CCN5 is a novel signaling molecule that critically participates in the mitogenic action of PMA on noninvasive, WISP-2/CCN5-positive breast tumor cells through PKCalpha-dependent, multiple molecular signal transduction pathways.
- We conclude that compound 48/80 is an effective activator of PI 3-kinase dependent pathways, leading to the activation of effectors including PKB/Akt, p70(S6K) and PKCalpha.
- Our data suggest that PKCalpha, but not PKCbeta, is the predominant cPKC isoenzyme required for cPLA(2) protein phosphorylation and maximal induction of cPLA(2) enzymatic activity upon activation of human monocytes.
- PCK-alpha activation in keratinocytes is a crucial event orchestrating cutaneous neutrophil responses.
- These results show for the first time that IP6 represses telomerase activity in prostate cancer cells by posttranslational modification of TERT via the deactivation of Akt and PKCalpha.
- NT uses PKC-dependent pathways to modulate GSK-3, which may play a role in the NT regulation of intestinal cell growth
- a functional contribution of PKCalpha to tamoxifen resistant growth of human breast cancer cells
- alpha-PKC and beta-PKC are required for optimal O(2)(-) generation, but play different roles in Ca2+ signaling for phagocytic responses such as O(2)(-) generation
- Data suggest that MCF-7 cell proliferation or the anti-cancer action of doxorubicin and vinblastine on breast cancer cells is independent of PKC-alpha.
- Galphaq activation of TRPC6 signals the activation of PKCalpha, and thereby induces RhoA activity and endothelial cell contraction
- These results suggest that different PKC isoforms may exert ontogenetic-specific functions in erythropoiesis and that modulation of PKCalpha might affect the activity of (A)gamma-promoter-driven reporters.
- Ras is able to promote monocyte lineage selection via PKC.
- Conventional PKC isoforms, especially PKCalpha, mediate feedback inhibition of G-protein-coupled receptor -induced EGFR transactivation.
- These data suggest that an intracellular calcium store independent PKC-Sp1 signaling pathway induces early keratinocyte differentiation through upregulation of TSG101.
- "PKCalpha-NF- kappaB"-dependent cascade is involved in the signaling leading to phorbol myristate acetate-induced matrix metalloproteinase-9 expression in the lung epithelium
- These data demonstrate that IGF-I induces COX-2 expression in human ovarian cancer cells, which is mediated by three parallel signaling cascades--PI3K, MAPK, and PKC pathways that differentially regulate COX-2 expression.
- the cell fate commitment of CD14(+)monocytes towards MDMs or MoDCs appears to be steered by the selective activation of PKCalpha or PKCbeta(I), respectively.
- Protein Kinase C alpha mRNA was significantly increased in human hepatocellur carcinomas as compared to corresponding non-cancerous liver tissues.
- STAT3 and PKC differentially regulate telomerase activity during megakaryocytic differentiation of K562 cells.
- HER2 overexpression in HER2 2+ carcinomas is associated with neither an increase in gene transcription nor a deregulation in the ubiquitin-dependent pathways, but instead seems to be regulated by protein kinase Calpha (PKCalpha) activity.
- Determination of PKC-alpha levels/activity in leukaemia seems to be relevant when choosing efficient chemotherapy protocols based on the use of apoptosis-inducing anticancer drugs.
- Differential phosphorylation of NG2 proteoglycan by ERK and PKCA helps balance cell proliferation and cell movement.
- analysis of direct binding and activation of PKCalpha and PKCdelta by steroid hormones and the molecular mechanisms involved
- PKC-alpha is the predominant conventional PKC present in the human coronary and skeletal microcirculation
- PKC alpha, rather than other protein kinase C isoforms, participates in lysophosphatidic acid-induced NF-kappa B activation and urokinase upregulation in ovarian cancer cells.
- Hemoglobin promptly and markedly modified the levels of expression of both calcium-dependent PKCalpha and calcium-independent PKCzeta.
- The protein kinase C (PKC) inhibitor and apoptotic inducer staurosporine switches the production of Bcl-x towards the x(S) mRNA isoform in 293 cells.
- These results suggest that the PKCalpha isoform is an important regulator of cell migration in response to agricultural dust exposure.
- Data show that expression of DMPK-CUG-repeat RNA results in hyperphosphorylation and stabilization of CUGBP1, and suggest that inappropriate activation of the PKC pathway contributes to the pathogenic effects of a noncoding RNA.
- findings provide the first evidence that stimulation of P-selectin surface expression via PKCalpha-dependent PKD2 activation could be an important mechanism in the early onset of AII-initiated endothelial adhesiveness.
- Study shows that activation of protein kinase C-alpha (PKC-alpha) phosphorylated and down-regulated LRP expression.
- Protein kinase C alpha promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor.
- Ro3582 inhibits cell proliferation and activates bone morphogenetic protein/Smad signaling via a Ras and PKC alpha pathway in breast epithelial cells.
- discrete PKCs trigger distinctive responses when activated in different phases of the cell cycle via a common mechanism that involves p21 Cip1 up-regulation.
- Moraxella catarrhalis infection activates protein kinase C and its isoforms alpha, epsilon and theta, which differentially regulate interleukin-8 transcription in human pulmonary epithelial cells.
- RXR ligands rapidly inhibit high-glucose-induced oxidative stress by antagonizing high-glucose-induced PKC activation, and cytoplasmic RXRalpha is implicated in this regulation
- In pancreatic tumor cells calcium-dependent PKC-alpha mediates TGF-beta-induced transcriptional downregulation of PTEN, and this pathway promotes cell migration in a SMAD4-null environment.
- Data show that NG2 and integrin alpha4 oppositely regulate anoikis in fibroblasts, and that NG2 and integrin alpha4 regulate FAK phosphorylation by PKCalpha-dependent and -independent pathways, respectively.
- Overexpression of protein kinase Calpha mRNA is associated with gastric carcinoma
- modulation of PKC may have therapeutic potential in the prevention of smoke-related lung injury
- A novel regulatory signaling mechanism of transcriptional control in which the LHR is derepressed through PKCalpha/ERK-mediated Sp1 phosphorylation, causing the release of HDAC1/mSin3A complex from the promoter.
- Thus, survivin, Smac, and PKC alpha might play important roles in the inhibition of apoptosis by FGF-2 in human small cell lung cancer cells.
- PKP2 knockdown is accompanied by increased phosphorylation of PKC substrates, raising the possibility that global alterations in PKC signaling may contribute to pathogenesis of congenital defects caused by PKP2 deficiency.
- These results suggest a significant role of PKCalpha and downstream actin filament activity during the fungal invasion into human brain microvascular endothelial cells.
- TRPV1 mediates heat shock-induced MMP-1 expression via calcium-dependent PKCalpha signaling in HaCaT cells
- A 46kDa variant of ERalpha increased in abundance in the cell membrane within 20 minutes of estradiol treatment suggesting that ERalpha mediated the estradiol non-genomic effects on PKCA through the formation of a membrane-associated signalling complex.
- A novel interferon-independent pathway involving protein kinase C (PKC)-alpha activation, upstream of p38 and c-jun N-terminal kinase, is responsible for poly (I:C) pro-apoptotic effects on LNCaP cells.
- Akt-mediated phosphorylation modulates eNOS uncoupling and greatly increases O(2)* generation from the enzyme at low Ca(2+) concentrations, and PKCalpha-mediated phosphorylation alters the sensitivity of the enzyme to other negative regulatory signals.
- PDGFR-mediated phosphorylation at this site is dependent on PKCalpha, a conventional PKC isoform implicated previously in disruption of adherens junctions.
- findings shed light on post-transcriptional regulation of HSP70 expression, suggesting a molecular cascade involving PKC/HuR/HSP70- that possibly represents an early event in the cellular response to oxidative stress in SH-SY5Y human neuroblastoma cells
- Protein kinase Calpha levels are elevated in the pregnant myometrium suggesting the involvement of protein kinase Calpha in regulation of human uterine contraction.
- ANG II inhibited hOAT1 activity through activation of PKCalpha, which led to the redistribution of the transporter from the cell surface to the intracellular compartments.
- These results demonstrated that in A549 cells, activation of p50/p65 heterodimer through sequential activation of PKC alpha-JNK-NIK-IKK beta-NF-kappaB was required for IL-1 beta-induced uPA expression associated with migration of tumor cells.
- p73 is able to induce cell cycle arrest independently of its amino-terminal transactivation domain, whereas this domain is crucial for p73 proapoptotic functions.
- EGFR signals to mTOR through PKC and independently of Akt in glioma