Additional Information:
accession Q92956|express systemHEK293|product tagC-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundHerpesvirus entry mediator (HVEM), also known as tumor necrosis factor receptor superfamily member 14 (TNFRSF14), is a human cell surface receptor of the TNF-receptor superfamily. Two TNF superfamily ligands lymphotoxin (TNF-) and LIGHT (TNFSF14) are identified as cellular ligands for HVEM and initiate the positive signaling.|molecular weightThe protein has a predicted MW of 18.5 kDa. Due to glycosylation, the protein migrates to 32-48 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Human HVEM/TNFRSF14 Protein 4355proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceHerpesvirus entry mediator (HVEM), also known as tumor necrosis factor receptor superfamily member 14 (TNFRSF14), is a human cell surface receptor of the TNF-receptor superfamily. Two TNF superfamily ligands lymphotoxin (TNF-) and LIGHT (TNFSF14) are identified as cellular ligands for HVEM and initiate the positive signaling.Protein namesTumor necrosis factor receptor superfamily member 14 (Herpes virus entry mediator A) (Herpesvirus entry mediator A) (HveA) (Tumor necrosis factor receptor-like 2) (TR2) (CD antigen CD270)Gene namesTNFRSF14,TNFRSF14 HVEA HVEM UNQ329/PRO509Protein familyTumor necrosis factor receptor superfamilyMass9606DaFunctionReceptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network (PubMed:10754304, PubMed:18193050, PubMed:23761635, PubMed:9462508). Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation (PubMed:19915044, PubMed:9153189, PubMed:9162022). Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions (PubMed:10754304). Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response (PubMed:23761635). In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and pro-inflammatory cytokines (By similarity). Upon binding to CD160 on activated CD4+ T cells, down-regulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (PubMed:18193050). May interact in cis (on the same cell) or in trans (on other cells) with BTLA (By similarity) (PubMed:19915044). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (By similarity) (PubMed:19915044).; (Microbial infection) Acts as a receptor for Herpes simplex virus 1/HHV-1.; (Microbial infection) Acts as a receptor for Herpes simplex virus 2/HHV-2.Subellular locationCell membrane ; Single-pass type I membrane protein .TissuesWidely expressed, with the highest expression in lung, spleen and thymus. Expressed in a subpopulation of B cells and monocytes (PubMed:18193050). Expressed in naive T cells (PubMed:19915044).StructureInteracts with TRAF2, TRAF3 and TRAF5 (PubMed:9153189, PubMed:9162022). Interacts (via CRD1/TNFR-Cys 1) with CD160; this interaction is direct (PubMed:18193050, PubMed:23761635). Interacts with LTA and TNFSF14 (PubMed:9462508). Interacts (via CRD1/TNFR-Cys 1) in cis and trans with BTLA; the cis interactions inhibits the trans interactions (PubMed:16169851, PubMed:19915044).; (Microbial infection) Interacts with herpes simplex virus 1/HHV-1 envelope glycoprotein D.; (Microbial infection) Interacts with herpes simplex virus 2/HHV-2 envelope glycoprotein D.Post-translational modificationN-glycosylated.DomainThTarget Relevance information above includes information from UniProt accession: Q92956The UniProt Consortium|