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Validated All-in-One™ qPCR Primer for TNFRSF14(NM_003820.3) Search again
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:
Summary
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor was identified as a cellular mediator of herpes simplex virus (HSV) entry. Binding of HSV viral envelope glycoprotein D (gD) to this receptor protein has been shown to be part of the viral entry mechanism. The cytoplasmic region of this receptor was found to bind to several TRAF family members, which may mediate the signal transduction pathways that activate the immune response. [provided by RefSeq].
Gene References into function
- Data suggest involvement of TNF superfamily receptor members and ligands in human atherosclerosis. TNFRSF14 (HVEM, TR2, LIGHTR)analysis, found this receptor in regions rich in CD68-positive macrophage-derived foam cells and HLA-DR-positive cells.
- Crystallization and preliminary diffraction studies of the ectodomain of the envelope glycoprotein D from herpes simplex virus 1 alone and in complex with the ectodomain of the human receptor HveA
- Data show that mRNA encoding LIGHT and its receptors [HVEM, LTbetaR, and TR6 (DcR3)] are present in placentas and cytotrophoblast cells at term.
- association of HVEM and nectin-1 with lipid rafts during herpes simplex virus entry
- sHVEM levels were elevated in sera of patients with allergic asthma, atopic dermatitis and rheumatoid arthritis
- both nectin 1 and HVEM receptors play a role during HSV infection in vivo and both are highly efficient even at low levels of expression
- HVEM binds to B T lymphocyte attenuator (BTLA), an Ig family member, which inhibits T cell proliferation.
- Binding of HVEM to BTLA attenuates T cell activation, identifying HVEM/BTLA as a coinhibitory receptor pair.
- in cells a complex forms through physical associations of HVEM, HSV-1 gD, and at least gH
- both LTbetaR and HVEM can discriminatively mediate the expression of different genes in cultured human umbilical vein endothelial cells, including LIGHT, a proinflammatory cytokine
- distinct herpesviruses target the HVEM-BTLA cosignaling pathway, suggesting the importance of this pathway in regulating T cell activation during host defenses.
- 2.8-A crystal structure of the BTLA-HVEM complex shows that BTLA binds the N-terminal cysteine-rich domain of HVEM and employs a unique binding surface
- Real-time RT-PCR confirmed up-regulation of IL-8, osteopontin, and TNFRSF14 and down-regulation of SAMeS and CD209 in AH.
- HVEM, a membrane-bound receptor that protects against apoptosis, was expressed only on syncytiotrophoblast
- HSV-1-gD-HveA interaction initiates a signal transduction pathway leading to NF-kappaB activation
- Ca(2+)is a downstream mediator of the LIGHT/HVEM interaction in monocytes
- CD160 serves as a negative regulator of CD4+ T cell activation through its interaction with HVEM.
- Expression of entry receptors nectin-1 and HVEM prevent entry of HSV-1 into human conjunctival epithelium.
- These results establish that HVEM is involved in NF-kappaB activation by herpes simplex virus 1 glycoprotein D.
- LIGHT-mediated upregulation of PAR-2 in endothelial cells is mediated through the HVEM receptor, involving Jun N-terminal kinase signaling pathways.
