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Validated All-in-One™ qPCR Primer for EIF2AK2(NM_002759.3) Search again
Product ID:
HQP014948
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
DYT33, EIF2AK1, LEUDEN, PKR, PPP1R83, PRKR
Gene Description:
eukaryotic translation initiation factor 2 alpha kinase 2
Target Gene Accession:
NM_002759.3(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:
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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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Gene References into function
- The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR (TCTP PROTEIN)
- IL-1beta and IL-10 interact with IFN-alpha to up- and down-regulate PKR gene expression, respectively, by modulating STAT1 activation induced by IFN-alpha
- Protein kinase R (PKR) regulates double-stranded RNA induction of TNF-alpha but not IL-1 beta mRNA expression in airway epithelial cells.
- PKR phosphorylates small delta antigen
- PKR protein kinase phosphorylation and dimerization is controlled byt PP1C
- PKR activated by direct binding in heparin-treated vascular smooth muscle cells (VSMCs)blocks G1- to S-phase transition.
- The induction of anti-HIV CTL activity by p9-RNA could be mediated by PKR through NF-kappaB activation
- PKR may assume multiple roles in modulating hepatitis C virus replication and protein synthesis
- Us11 protein of herpes simplex virus type 1 can block PKR activation by PACT both in vitro and in vivo
- The promoter-proximal KCS element of the PKR kinase gene enhances transcription irrespective of orientation and position relative to the ISRE element.
- PRK activity is suppressed by HSP70 in cooperation with FANCC
- PKR binds to ASK1 and is involved in apoptosis signalling pathways
- PKR upregulation occurs at defined steps in cancer progression, probably as a cellular response to neoplasia
- overexpression of NPM suppressed PKR activity, enhanced protein synthesis, and inhibited apoptosis. Fanconi anemia lymphoblasts expressed low levels of NPM, which correlated with high ground-state activation of PKR and hypersensitivity to apoptotic cues
- Polymorphisms in the interferon-inducible elF2alpha kinase gene is associated with outcome of hepatitis C virus infection
- In contrast to nondemented controls, Alzheimer cases show prominent protein kinase PKR activation in association with neuritic plaques and pyramidal neurons in the hippocampus and neocortex.
- PKR is overexpressed in hepatitis C virus related hepatocellular carcinoma.
- viral-induced PKR activation may play a significant role in pathogenesis by mediating the host response to poliovirus encephalitis
- PKR might play a role in ER stress-induced apoptosis and in Alzheimer's disease.
- Loss of PKR activity may contribute to the formation and/or maintenance of B-cell chronic lymphocytic leukemia
- TRAF-PKR interaction model in which the C-terminal domain of TRAF binds to a predicted TRAF interaction motif present in the PKR kinase domain.
- level of PKR reduced in hepatocellular carcinoma tumor tissues, suggesting a role in promoting tumor growth; hepatitis B virus may participate in altering the level of PKR, but other factors should play a more determining role in regulation of PKR in HCC
- Inappropriaate activation of PKR may cause mutations in fanconi anemia proteins.
- upregulated in liver and PMBCs of chronic hepatitis C patients, and nonresponsivenes to IFN-alpha treatment is associated with this upregulation. The PKR gene response to exogenous IFN was similar in responders and non-responders in PBMCs.
- phosphyorylation inhibited by Epstein-Barr virus BILF1 protein
- first detection of a mutation in the RNA-binding domains of PKR gene from tumor cells taken directly from patients
- double-stranded RNA-dependent protein kinase/eukaryotic initiation factor-2alpha has a role in okadaic acid-induced apoptosis in human osteoblastic MG63 cells
- results support the hypothesis that PKR phosphorylation of Tat may be important for its function in HIV-1 LTR transactivation
- hepatocarcinoma core positive cells are characterized by a significant PKR phosphorylation in Thr 446 residue, which leads deregulation of mitosis
- PKR may play a critical role in mediating the subversive effects of HIV Tat resulting in IL-10 induction
- results do not support the concept of PKR as a tumor suppressor in small-size peripheral adenocarcinomas of the lung
- in the absence of IFN treatment, activation of PKR basal expression is mediated by Sp1 and Sp3 proteins in a cooperative manner
- HCV core expression leads to deregulation of the mitotic checkpoint via a p38/PKR-dependent pathway
- We demonstrated that the direct binding of the influenza A virus NS1A protein to the N-terminal 230 amino acid region of PKR inhibits PKR activation by PACT and dsRNA
- interaction between PKR and dsRNAs represents a crucial host cell defense mechanism against viral infection
- These observations suggest a model for PKR activation upon binding of dsRNA or PACT.
- RAX may function as a negative regulator of growth that is required to activate PKR in response to a broad range of apoptosis-inducing stress.
- PKR differentially regulates TNF signaling; IKK, Akt and JNK were positively regulated, whereas p44/p42 MAPK and p38 MAPK were negatively regulated.
- levels of PKR in lymphocytes could follow the cognitive decline in Alzheimer's disease
- Protein kinase R is involved in NF-kappaB mediated gene transcription of pro-inflammatory cytokines via IkappaB kinase-beta.
- the salt bridge interaction and dimer interface observed in the PKR structure is critical for the activity of PKR, GCN2, and PERK
- kinase domains is critical in the propagation of the activation signal and for PKR dimerization
- PKR tyrosine phosphorylation provides an important link between IFN signalling and translational control through the regulation of eIF2alpha phosphorylation.
- the effects of PKR on the replication cycle of parainfluenza virus type 5
- Phosphorylation of translation initiation factor 2-alpha (eukaryotic initiation factor 2-alpha (eIF2-alpha)) and its kinase, PKR, occur in dsRNA-induced apoptosis but not in necrosis.
- The present work analyses another gene involved in the host cell response to HSV-1, EIF2AK2 (eukaryotic translation initiation factor 2-alpha kinase 2.
- PKR can function to control cell growth and cell differentiation, and its activity can be controlled by the action of several oncogenes [review]
- Data suggest that protein kinase PKR plays a stimulus- and virus-dependent role in apoptotic death and virus multiplication in human cells.
- The putative dsRNA receptor PKR may not play a pivotal role in the dsRNA-stimulated expression of inflammatory chemokines in airway epithelial cells.
- it appears that HCV protein expression is directly dependent on PKR expression; PKR is antiviral toward HCV and responsible for IFN's effect against HCV.
- The effects of ribavirin plus interferon alpha (IFN-alpha) on EIF2AK2 activity were greater than those observed for treatment with either ribavirin alone or IFN- alpha alone.
- These results suggest that a novel mechanism other than endoplasmic reticulum(ER) stress element-dependent mRNA transcription is required for induction of GRP94 and phosphorylation of PKR contributes to the induction of GRP94 under ER stress.
- PKR was not necessary for Sendai virus-induced IFN synthesis, suggesting that PKR is particularly important for recognition of WNV infection
- These results indicate that the endoplasmic reticulum-stress-mediated eIF2alpha/ATF4/CHOP/cell death pathway is, to some degree, dependent on PACT-mediated PKR activation apart from the PERK pathway.
- PKR activates glycogen synthase kinase 3 to promote the proteasomal degradation of p53.
- Airway smooth muscle cells expressed PKR but it did not seem to be involved in poly I:C effects on muscarinic receptors.
- this study suggests that the role played by non-coding T cells transcript in the activation of lymphocytes can be mediated by PKR through NF-kappaB activation
- study provides evidence that double-stranded RNA-activated protein kinase (PKR), a stress kinase, is involved in HIV/gp120-associated neurodegeneration
- the single-cycle yield of delta-E3L virus was increased by nearly 2 log10 in PKR-deficient cells over the impaired growth in PKR-sufficient cells.
- the paramyxovirus P/V gene products limit induction of PKR by limiting the synthesis of aberrant viral mRNAs and double-stranded RNA and thus prevent the shutdown of translation
- PrP aggresomes initiate a cell stress response by activating the RNA-dependent protein kinase (PKR).
- study reports that RNAs with very limited secondary structures activate PKR in a 5'-triphosphate-dependent fashion in vitro and in vivo
- PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation
- Phosphorylation of PKR may be an important initiator of muscle wasting in cancer patients.
- PKR activation by ssRNA and dsRNA containing internal nucleobase, sugar, and phosphodiester modifications was analyzed.
- this protein kinase could be involved in the pathogenesis of myelodysplastic sysdromes
- Double-stranded RNA-activated protein kinase mediates induction of interleukin-8 expression by deoxynivalenol, Shiga toxin 1, and ricin in monocytes.
- Results demonstrate that the Sendai virus C protein limits generation of double stranded RNA, thereby keeping protein kinase R inactive to maintain intracellular protein synthesis.
- Epidermal keratinocytes efficiently respond to viral double-stranded dsRNA equivalent poly(I:C) by expressing protein kinase R (PKR) dsRNA sensing molecules together with their downstream signaling pathway in a functional and differentially regulated way
- NS5A protein down-regulates the expression of spindle gene Aspm through PKR-p38 signaling pathway
- These data provide the first evidence identifying Nck-1 as a novel endogenous regulator of PKR and support the notion that Nck-1-PKR interaction could be a way to limit PKR activation.
- PKR facilitates the host innate immune response and apoptosis in virus-infected cells by mediating IRF-3 activation through the mitochondrial IPS-1 signal transduction pathway
- TRBP controls PACT activation of PKR, an activity that is reversed by stress.
- PKR regulates B56(alpha)-mediated BCL2 phosphatase activity in acute lymphoblastic leukemia-derived REH cells.
- These results indicated that oxidative stress induces PKR expression essentially via the IFN-gamma activation signal, and causes apoptosis in Jurkat T cells.
- These results indicate that PKR plays an important antiviral role during measles virus infection but that the virus growth restriction by PKR is not dependent upon the induction of apoptosis.
- PKR, in addition to IPS-1 and IRF3 but not TRIF, was required for maximal type I IFN-beta induction and the induction of apoptosis by both transfected PRNAs and polyinosinic-polycytidylic acid.
- Inhibition of PKR in SARS-CoV-infected cells does not affect viral replication. SARS-CoV infection activates PKR and PERK, leading to sustained eIF2alpha phosphorylation. Viral activation of PKR can lead to apoptosis.