|
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 RIGI(NM_014314.3) Search again
Product ID:
HQP006239
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
DDX58, RIG-I, RIG1, RLR-1, SGMRT2
Gene Description:
RNA sensor RIG-I
Target Gene Accession:
NM_014314.3(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
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. This gene encodes a protein containing RNA helicase-DEAD box protein motifs and a caspase recruitment domain (CARD). It is involved in viral double-stranded (ds) RNA recognition and the regulation of immune response. [provided by RefSeq].
Gene References into function
- IFN-gamma induces the expression of RIG-I, which may play a role in the immunological effects of IFN-gamma
- RIG-I may play some pathophysiological role in immune and inflammatory reactions in vascular smooth muscle cells(SMC).
- Although the physiological function of RIG-I is still unknown, induction of RIG-I by IFN-gamma may play an important role in inflammatory or immunological reactions in endothelial cells.
- hepatocytes contain two distinct antiviral signaling pathways leading to expression of intereron beta, one dependent upon TLR3 and the other dependent on RIG-I, with little cross-talk between these pathways
- Importantly, we show that NS3/4A can strongly inhibit the ability of the recently described RIG-I protein to activate IFN, suggesting that RIG-I is a key factor in the TRIF-independent, NS3/4A-sensitive pathway.
- Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity.
- Cardif functions as an adaptor, linking the cytoplasmic dsRNA receptor RIG-I to the initiation of antiviral programs
- JEV and DEN-2 initiate the host innate immune response through a molecular mechanism involving RIG-I/IRF-3 and PI3K/NF-kappaB signaling pathways
- the virus-inducible, NF-kappaB-dependent activation of A20 functions as a negative regulator of RIG-I-mediated induction of the antiviral state
- HCV infection transiently induces RIG-I- and IPS-1-dependent IRF-3 activation
- HCV blocks the RIG-I-mediated dsRNA signaling by an NS3/4A-independent mechanism, in addition to the NS3/4A-dependent cleavage of MAVS/IPS-1.
- In conclusion, our results show that in epithelial cells influenza A virus-induced antiviral cytokine gene expression is triggered by RIG-I and mda-5, whose expression is positively regulated by IFN-alpha.
- EBERs activated RIG-I's substrates, NF-kappaB and IFN regulatory factor 3, which were necessary for type I IFN activation.
- results identify RIG-I as a ssRNA sensor and potential target of viral immune evasion and suggest that its ability to sense 5'-phosphorylated RNA evolved in the innate immune system as a means of discriminating between self and nonself
- findings demonstrated that the 5'-triphosphate end of RNA generated by viral polymerases is responsible for retinoic acid-inducible protein I (RIG-I)-mediated detection of RNA molecules
- We now report that the NS1 of influenza A virus interacts with RIG-I and inhibits the RIG-I-mediated induction of IFN-beta.
- RIG-I might operate not only as a RNA helicase but also as a mediator of the cytokine network in the inflammatory skin diseases, such as psoriasis vulgaris
- In this review, RIG-I has evolved an immune surveillance system for antiviral responses by its detection and direct binding to the 5'-end of certain viral RNA genomes, specifically, to a 5'-triphosphate group.
- The putative dsRNA receptor RIGI may not play a pivotal role in the dsRNA-stimulated expression of inflammatory chemokines in airway epithelial cells.
- RNA helicase cytoplasmic sensor RIG-I mediates innate antiviral signaling that is not inhibited by dihydroxyacetone kinase.
- TNF-alpha leads to stabilization of IFN-epsilon mRNA, increased IFN-epsilon synthesis, engagement of type I IFNRs, increased STAT1 expression and phosphorylation, and up-regulation of retinoic acid-inducible gene-I expression
- RIG-I is an essential component of the pathway relevant to polyinosinic-polycytidylic acid signaling of type I interferon in intestinal epithelial cells.
- Our results show that PAMP receptors, TLR3, TLR7 and RIG-I mRNA levels are significantly down-regulated in patients with chronic hepatitis C infection when compared with healthy controls.
- RIG-I may be involved in the inflammatory reaction in pericardial mesothelial cells.
- Data show that the C-terminal domain (CTD) of RIG-I recognizes two distinct viral RNA patterns: double-stranded (ds) and 5'ppp single-stranded (ss), and suggest that the bipartite structure of CTD regulates RIG-I on encountering viral RNA patterns.
- A RIG-I/IFNalphabeta receptor (IFNAR)1-dependent pathway mediates SOCS1 and SOCS3 up-regulation in influenza A virus-infected bronchial epithelial cells.
- Data show that RIG-I mRNA and protein are expressed in HeLa cells stimulated with IFN-gamma, and that RNA interference against RIG-I results in the suppression of IFN-gamma-induced CXCL11 expression.
- innate cytokine responses in myeloid dendritic cells are impaired regardless of enhanced expressions of TLR2, TLR4, and RIG-I in HCV infection
- These results establish RIG-I as a major intracellular recognition receptor for the genome of most negative-strand RNA viruses.
- RIG-I-mediated co-induction of TNF and type I IFN by virus-infected primary human macrophages represents a novel innate defense mechanism to restrict viral infection in human cells.
- role of the intact tandem CARD for TRIM25-mediated RIG-I activation; RIG-I splice variant is an off-switch regulator of its own signaling pathway.
- identify an alternative factor, Riplet/RNF135, that promotes RIG-I activation independent of TRIM25
- It has nonself RNA sensing mechanism and functions as a virus sensor.
- gC1qR is a physiological inhibitor of the RIG-I and MDA5-mediated antiviral signaling pathway