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Validated All-in-One™ qPCR Primer for PRKCB(NM_212535.2) Search again
Product ID:
HQP054928
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
PKC-beta, PKCB, PKCI(2), PKCbeta, PRKCB1, PRKCB2
Gene Description:
protein kinase C beta
Target Gene Accession:
NM_212535.2(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 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 protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption.
Gene References into function
- Investigation of the inhibitory effects of chelerythrine chloride on the translocation of the protein kinase C betaI, betaII, zeta in human neutrophils
- PKC-beta 1 when activated enhances calcium flux and protects the assembly of the F-actin cytoskeleton in intestinal monolayers against oxidants.
- A method that uses liquid chromatography electrospray ionization-mass spectrometry to quantify site-specific protein phosphorylation was used to measure the time-dependent increase of phosphorylation by PRKCB2 at a PKC-preferred site, Ser44.
- PKC beta II 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.
- The turn motif is a phosphorylation switch that regulates binding of Hsp70.
- REVIEW:Interaction of protein kinase C isozymes with membranes containing anionic phospholipids utilizing fluorescent phorbol esters to probe the properties of the C1 domains
- Nephroprotective actions of the ACE inhibitor lisinopril in experimental diabetes mellitus were associated with and thus could be mediated in part by inhibition of diabetes-induced activation of PKC beta isoenzymes in the renal cortex.
- PKCbeta has a role in in the chemotactic response of human monocytes to MCP-1
- elevated glucose increases the activity of core 2 GlcNAc-T and adhesion of human leukocytes to retinal capillary endothelial cells, in a dose-dependent manner, through diabetes-activated serine/threonine protein kinase C beta2 dependent phosphorylation
- DNA sequence differences in the promoter of PRKCB1 contribute to diabetic nephropathy susceptibility in type I diabetes mellitus
- data indicate a highly specific function of PKCbeta for regulation of TCR-CD28 induced-signaling, IL-2 gene expression and secretion in Jurkat T cells
- PKCalpha and betaII have roles in the regulation of membrane recycling
- protein kinase Cbeta is a direct, downstream target of RUNX1
- EGF-mediated protection against oxidant disruption of the intestinal barrier function requires PKC-beta1 activation and NF-kappaB suppression.
- These results suggest that phosphorylation of tyrosinase by PKC-beta induces a complex formation between tyrosinase and TRP-1.
- PKCbetaII induces cell invasion through a Ras/Mek-, PKC iota/Rac 1-dependent signaling pathway
- phospholipase D causes translocation of protein kinase C (PKC)betaII but not PKCbetaI to a juxtanuclear subset of recycling endosomes
- RACK-I anchors activated PKC-beta on the melanosome membrane, allowing PKC-beta to phosphorylate tyrosinase
- Protein kinase CbetaII regulates its own expression in rat intestinal epithelial cells and the colonic epithelium in vivo.
- PKC-MAPK pathway mRNAs plays an important role in the development and/or progression of early tissue damage in diabetic nephropathy
- results showed that PKC beta(II) and delta isozymes are essential for the activation of IL-10 production in human monocytes following stimulation by HIV-1 Tat protein
- We analyzed the dependence of the expression of some selected protein kinase C isoenzymes on the availability and/or action of androgens.
- juxtanuclear translocation of protein kinase C betaII is selectively inhibited by a negative feedback mechanism involving ceramide formed from the salvage pathway
- Chemotaxis to PDGF-BB in 25 mmol/L glucose is PKCbetaII-dependent and requires activation of both the PI3K and MAPK pathways.
- PKCbetaII is regulated by PI 3-kinase in HT29 cells
- the level of Smad6s can alter the level of TGF-beta and the subsequent induction of PAI-1 via a FoxD1 transcription site
- This evidence supports that the Hal gene is turned on by glucocorticoids and by glucagon either via PKC or PKA, but prefers the PKA pathway.
- Inhibition of protein phosphatase 2A increased phosphorylation at Ser660 that determines calcium sensitivity and activity of protein kinase c betaII isoform
- Regulation of protein kinase C betaII expression and signaling play critical roles in mediating progenitor to dendritic cell differentiation
- PRKCB1 gene on chromosome 16p may be involved in the etiology of autism.
- The data do not support a strong association between single nucleotide polymorphism of PRKCB and spina bifida risk.
- Furthermore, curcumin strongly repressed the PMA-induced phosphorylation of ERK, JNK, and p38 MAP kinase, which were dependent on the PKC pathway
- Acrosomal exocytosis is regulated through the PKC-mediated phosphorylation of conserved threonines in the polybasic regions of synaptotagmin VI.
- Data show that activity of protein kinase B in hormone-dependent mammary tumors was significantly higher than in tumor tissue from patients with negative receptor status.
- A novel mechanism by which ROS can initiate cell death through the activation of PKC-betaI is reported.
- Protein kinase C can inactivate TRPC3 indirectly by activating protein kinase G, and directly by phosphorylation on Ser-712.
- Protein kinase Calpha, betaI, and betaII isozymes regulate cytokine production in mast cells through MEKK2/ERK5-dependent and -independent pathways.
- Subcellular localization of protein kinase C (PKC)-beta, CD81, and LFA-1 was determined in T lymphocytes.
- 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
- study indicates that PRKCB1 is a predictor for worsening of kidney disease in Japanese subjects with type 2 diabetes
- Thus PKC-beta2 is hypothesized to participate in the regulation of CFTR apical plasma membrane targeting within the constitutive cellular biosynthetic pathway.
- PKC-beta-dependent augmentation of transcellular ISC-cAMP at the level of the basolateral membrane demonstrated that transport events with geographically distinct subcellular membranes can be independently regulated by the PKC beta-isoform.
- These results indicate that Hcy (homocysteine)-stimulated superoxide anion production in monocytes is regulated through PKC-dependent phosphorylation of p47phox and p67phox subunits of NADPH oxidase.
- 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
- Incubation of podocytes with membranous glomerulonephritis sera determined strong upregulation of pPKC-alpha/beta that was reverted by pre-incubation with clusterin
- Data describe the role of angiotensin II type 1A receptor phosphorylation, phospholipase D, and extracellular calcium in isoform-specific protein kinase C membrane translocation responses.
- The suppressive effects on MDR3 mRNA of PMA were attenuated in antisense PKCbeta-treated cells. PKCbeta plays a regulatory role in the expression of MDR3.
- beta and some other PKC isoenzyme, most likely delta, mediate cholesterol accumulation when macropinocytosis of LDL is stimulated in PMA-activated human monocyte-derived macrophages
- overexpressed active PKCbetaII plays a role in the regulation and outcome of BCR signals that can be important for the progression of CLL
- structure of the Rac1-PLC-beta2 complex reveals determinants that dictate selectivity of PLC-beta isozymes for Rac GTPases over other Rho-family GTPases
- Findings indicate that IL-1beta-induced Cox-2 expression in human myometrial smooth muscle cells is dependent on the action of atypical PKCs, through stimulation of the activity of NF-kappaB.
- Data do not support the finding that the PRKCB1 gene variants contribute risk for the development of autism.
- hBVR activation of PKC betaII underscores its potential function in propagation of signals relayed through PKCs
- 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.
- PTH induces an increased activity of the eNOS system through PKA and PKC pathways
- HGF signaling process from Gab1 to PI3K is negatively regulated by PKC-betaII, and its loss is critical for melanoma cells to gain invasive potential.
- the compartmentalization of HLA-DR/CD18 complex within or outside lipid rafts as a mechanism through which HLA-DR can integrate both PTK and PKCbeta signals leading to activation and death
- Differential protein kinase C isoform abundance was observed in thoracic aortic aneurysm samples from patients with bicupsid valve versus those with tricupsid valve, suggesting independent molecular signaling pathways may be operative.
- PKC-beta I and II are differently distributed in the two prognostic subgroups of de novo diffuse large B-cell lymphoma.
- 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.
- the -546 polymorphism in the PKCbeta promoter reduces promoter activity, which leads to a decreased expression of PKCbeta2 and subsequently is associated with decreased peripheral insulin-dependent glucose uptake
- PLCgamma-mediated activation of PKCepsilon and PKCbetaI and intracellular calcium is involved in EGF-mediated protection of tight junctions from acetaldehyde-induced insult
- Data suggest that foreign body giant cell formation is supported by PKCbeta, PKCdelta, and PKCzeta in combined diacylglycerol-dependent (PKCbeta and PKCdelta) and -independent (PKCzeta) signaling pathways.
- discrete PKCs trigger distinctive responses when activated in different phases of the cell cycle via a common mechanism that involves p21 Cip1 up-regulation.
- The phosphorylation of ERK(1/2) and p38 MAPK was regulated by upregulated protein kinase C beta (PKC beta) in hepatocellular carcinoma.
- Cx43Hc electrical conductance is inhibited after PKC activation. Inhibition is predominantly mediated by PKC-epsilon. Partial inhibition may be provided by PKC-beta II/PKC-delta.
- PKC-beta is upregulated at the gene expression level in human diabetic nephropathy.
- Probiotic-secretory proteins protect the intestinal epithelium from hydrogen peroxide-induced insult by a PKC beta1/epsilon- and ERK1/2-dependent mechanism.
- the E3 activity of RBCK1 is controlled by two distinct manners, interaction with RBCK2 and phosphorylation by PKCbeta
- These findings demonstrate a central role for PKC-beta, and particularly PKC-betaII in the development of tubulointerstitial fibrosis.
- PKC delta in preeclamptic placentas promotes Bax dissociation from 14-3-3 zeta through 14-3-3 zeta phosphorylation.
- PRKCB2 (protein kinase C beta2) and PKCdelta (protein kinase C delta) counter-regulate coronary endothelial barrier properties by targeting distinctive subcellular sites.
- Taken together the results of the present study show that PKCbetaII can act as a specific PKC isoform regulating translation, in an mTOR-independent fashion, possibly close to the ribosomal machinery.
- ApoCIII activates PKCbeta, which inhibits the IRS-1/PI3K/Akt/eNOS pathway and induces endothelial dysfunction.
- Upregulation of PKCbetaII is associated with increased angiogenesis and prostate tumor cell proliferation
- protein kinase C betaII augments NF-kappaB-mediated TNF-alpha-induced transcription of the target gene CCL11, promoting p65 association with the CCL11 promoter, in human airway smooth muscle cells by phosphorylating p300/CBP-associated factor
- These data show that native ribosomes host active PKC and hence allow the phosphorylation of ribosome-associated substrates like initiation factors and mRNA binding proteins.
- Nonspecific inhibition of PKCbeta prevents LDL uptake in macrophages. These findings suggest that PKCbeta inhibitors may represent a novel class of antiatherosclerotic drugs.