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Validated All-in-One™ qPCR Primer for RIPK1(NM_003804.5) Search again
Product ID:
HQP021492
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AIEFL, IMD57, RIP, RIP-1, RIP1
Gene Description:
receptor interacting serine/threonine kinase 1
Target Gene Accession:
NM_003804.5(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
- cells pre-stimulated through TNFR-2 prior to subsequent activation of TNFR-1, showed enhanced cell death and recruitment of RIP to the TNFR-1 complex; deficiency of RIP rescued the infected cells from TNF-induced cytotoxicity
- FAK overexpression in human tumors provides a survival signal function by binding to RIP and inhibiting its interaction with the death receptor complex.
- RIP-dependent recruitment of MEKK3 plays a specific role in TNF-alpha signaling.
- TAK1 is recruited to the TNF-R1 complex via RIP and likely cooperates with MEKK3 to activate NF-kappaB in TNF-alpha signaling
- This study provides the first genetic evidence that the ubiquitination of RIP is required for TNFalpha-induced NF-kappaB activation.
- Activation of IKK by TNF-alpha requires site-specific ubiquitination of RIP1.
- TRADD and RIP1 compete for recruitment to the TNFR1 signaling complex and the distinct programs of cell death.
- RIP is one of the critical components involved in mediating DNA damage-induced, p53-independent cell death
- The expression of receptor-interacting protein 1 (RIP1) in peripheral blood mononuclear cells was significantly decreased in SLE patients.
- RIP may serve as a general activator of IRF7, responding to and transmitting the signals from various stimuli, and that ubiquitination may be a general mechanism for enhancing the activity of IRF7.
- We describe how RIP1 acts as a key integrator of signalling pathways initiated by stimulation of death receptors, bacterial or viral infection, genotoxic stress and T-cell homeostasis.
- findings show ubiquitination of RIP1 inhibits TNF-induced apoptosis first through an NF-kappaB-independent mechanism, then through an NF-kappaB-dependent mechanism; in absence of ubiquitination, RIP1 serves as a proapoptotic signaling molecule
- TNF-induced TRAF2-RIP1-AIP1-ASK1 complex formation and for the activation of ASK1-JNK/p38 apoptotic signaling.
- TNFRSF is upregulated after radical prostatectomy for prostatic neoplasms.
- RIP and c-FLIP-mediated assembly of the death-inducing signaling complex in nonrafts is a critical upstream event in TRAIL resistance
- These results suggested that HPB-ALL cells have a caspase-independent RIP kinasedependent pathway for Fas ligation.
- In response to autocrine TNFalpha signaling, the Smac mimetic promotes formation of a RIPK1-dependent caspase-8-activating complex, leading to apoptosis
- Data demonstrated that CK1alpha interacted with and phosphorylated RIP1 at the intermediate domain. Finally, we showed that CK1alpha enhanced RIP1-mediated NF-kappaB activation.
- Cezanne forms a novel negative feedback loop in pro-inflammatory signaling and that it suppresses NF-kappaB activation by targeting RIP1 signaling intermediaries for deubiquitination
- cytomegalovirus M45 protein provides a direct cell type-dependent replication benefit to the virus while modulating other biological processes signaling via the RIP1 adaptor such as activation of Toll-like receptor (TLR)3 and other mediators of cell deat
- activation and formation of TICAM-1 signalosomes with NF-kappaB and interferon regulatory factor-3 requires oligomerization induced at two different sites and RIP1 binding
- cIAP1 and cIAP2 promote cancer cell survival by functioning as E3 ubiquitin ligases that maintain constitutive ubiquitination of the RIP1 adaptor protein.
- c-IAP1 and c-IAP2 are required for TNFalpha-stimulated RIP1 ubiquitination and NF-kappaB activation.
- The protein encoded by the hybrid transcript lacks the putative kinase domain of RIP1, but potently stimulates NFkappaB, AP-1 and Ets-1 activity.
- the simultaneous downregulation of uPAR and MMP-9 induces apoptosome-mediated apoptosis through FADD-associated protein RIP and caspase 9
- Induction of NF-kappa B depends upon the adaptor receptor-interacting protein kinase (RIP)1, acting via a RIP homotypic interaction motif-dependent interaction with DNA-dependent activator of IFN regulatory factors (DAI).