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The protein encoded by TNFRSF14 is a member of the TNF-receptor superfamily. Additionally we are shipping TNFRSF14 Antibodies (184) and TNFRSF14 Kits (10) and many more products for this protein.
Showing 10 out of 29 products:
Human TNFRSF14 Protein expressed in Insect Cells - ABIN2666456
Pasero, Speiser, Derré, Olive: The HVEM network: new directions in targeting novel costimulatory/co-inhibitory molecules for cancer therapy. in Current opinion in pharmacology 2012
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Cynomolgus TNFRSF14 Protein expressed in Human Cells - ABIN2009868
Montgomery, Warner, Lum, Spear: Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. in Cell 1996
Show all 4 references for ABIN2009868
Human TNFRSF14 Protein expressed in Human Cells - ABIN2002597
Marsters, Ayres, Skubatch, Gray, Rothe, Ashkenazi et al.: Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB ... in The Journal of biological chemistry 1997
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Mouse (Murine) TNFRSF14 Protein expressed in CHO Cells - ABIN2003074
Schneider, Potter, Ware: Lymphotoxin and LIGHT signaling pathways and target genes. in Immunological reviews 2004
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Human TNFRSF14 Protein expressed in Human Cells - ABIN2002595
Cheung, Humphreys, Potter, Norris, Shumway, Tran, Patterson, Jean-Jacques, Yoon, Spear, Murphy, Lurain, Benedict, Ware: Evolutionarily divergent herpesviruses modulate T cell activation by targeting the herpesvirus entry mediator cosignaling pathway. in Proceedings of the National Academy of Sciences of the United States of America 2005
Show all 4 references for ABIN2002595
In eight cases (42%) we observed recurrent copy number loss of chr1:2,352,236-4,574,271, a region containing the candidate tumor suppressor TNFRSF14.
Study report the crystal structure of unbound HVEM, which further contributes to the understanding of the molecular mechanisms controlling recognition between HVEM and its ligands.
HVEM may play a critical role in tumor progression and immune evasion
Data indicate that tumour-expressing herpes virus entry mediator (HVEMplays a critical role in hepatocellular carcinoma (HCC (show FAM126A Proteins)), suggesting targeting HVEM may be a promising therapeutic strategy for HCC (show FAM126A Proteins).
Relative expression of HVEM and LTbetaR modulates canonical NF-kappaB (show NFKB1 Proteins) and pro-apoptotic signals stimulated by LIGHT.
Sequencing of TNFRSF14 located in the minimal region of loss in 1p36.32 showed nine mutations in pediatric follicular lymphoma.
HVEM plays a critical role in both tumor progression and the evasion of host antitumor immune responses, possibly through direct and indirect mechanisms.
HVEM gene polymorphisms are associated with sporadic breast cancer in Chinese women.
The conformation of the N-terminus of herpes simplex virus gD is induced by direct binding to HVEM and nectin-1 (show PVRL1 Proteins).
HVEM functions as a regulator of immune function that activates NK cells via CD160 (show CD160 Proteins) and limits lymphocyte-induced inflammation via association with B and T lymphocyte attenuator (show BTLA Proteins)
we identified herpes virus entry mediator as a functional receptor that mediates SALM5 (show LRFN5 Proteins)'s suppressive function. Our findings reveal a molecular link between the neuronal system and the immune system, and provide potential therapeutic targets for the control of CNS diseases.
results have revealed a novel role of HVEM on the regulation of IFN-I and immunopathology during Listeria infection.
our studies revealed a novel function of the HVEM cosignaling molecule and its ligands in EAU pathogenesis through the induction of Th1 (show HAND1 Proteins)- and Th17-type T cell responses
Together, these data indicate that HVEM contributes to ocular pathogenesis independently of entry and point to an immunomodulatory role for this protein specifically on radiation-resistant cells.
results demonstrate a role for both nectin-1 (show PVRL1 Proteins) and HVEM as receptors and suggest a further receptor which appears much less efficient.
Authors show that CD4 (show CD4 Proteins)(+) FoxP3 (show FOXP3 Proteins)(+) Tregs up- regulate HVEM (herpes virus entry mediator), which is a binding site for major viral glycoprotein gD, following herpes simplex virus 1 infection.
results support a model whereby BTLA (show BTLA Proteins) on innate leukocytes is triggered by HVEM and delivers negative signals into BTLA (show BTLA Proteins)(+) cells, thereby interfering with the protective immune response to this intestinal parasite.
In summary, herpes simplex virus 1 entry into epidermis was shown to strongly depend on the presence of nectin-1 (show PVRL1 Proteins), but the restricted presence of HVEM can potentially replace nectin-1 (show PVRL1 Proteins) as a receptor.
One mechanism by which the herpes simplex virus 1 latency-associated transcript enhances latency and reactivation appears to be by upregulating HVEM expression.
Data indicate taht tumor necrosis factor receptor superfamily member 14 (TNFRSF14)participated in ovariectomy (OVX)-induced adipose tissue (AT) inflammation via upregulation of CD11c (show ITGAX Proteins), resulting in metabolic perturbation.
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.
tumor necrosis factor receptor superfamily member 14
, tumor necrosis factor receptor superfamily, member 14 (herpesvirus entry mediator)
, herpesvirus entry mediator A
, CD40-like protein
, herpes virus entry mediator A
, tumor necrosis factor receptor-like 2
, tumor necrosis factor receptor-like gene2
, herpes virus entry mediator