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Recombinant Human Tumor necrosis factor receptor superfamily member 14 (TNFRSF14), partial (Active)

Recombinant Human Tumor necrosis factor receptor superfamily member 14 (TNFRSF14), partial (Active)

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Code: CSB-MP842173HU

Rate （5.0）
Review （1）

Size:

20ug100ug1mg

US$116

Quantity:

Express system: Mammalian cell

Species: Homo sapiens (Human)

Tag Info: C-terminal hFc1-tagged

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Target Background

Product Details

Abbreviation

Recombinant Human TNFRSF14 protein, partial (Active)

Purity

Greater than 90% as determined by SDS-PAGE.

Endotoxin

Less than 1.0 EU/ug as determined by LAL method.

Activity

Measured by its binding ability in a functional ELISA. Immobilized TNFRSF14 at 5 μg/ml can bind human TNFSF14(CSB-MP023991HUj2), the EC₅₀ is 49.85-79.31 ng/ml.②Measured by its binding ability in a functional ELISA. Immobilized human TNFRSF14 at 5 μg/ml can bind Biotinylated human TNFSF14 (CSB-MP023991HUj7-B), the EC₅₀ is 1.773-3.707 ng/ml.

Target Names

TNFRSF14

Uniprot NO.

Q92956

Research Area

Cancer

Alternative Names

HVEML; ATAR; CD270; CD40 like protein precursor; Herpes virus entry mediator A; Herpesvirus entry mediator A; Herpesvirus entry mediator; Herpesvirus entry mediator ligand; HveA; HVEM; HVEM L; LIGHT; LIGHTR; TNFRSF14; TNFSF 14; TNR14_HUMAN; TR2; Tumor necrosis factor receptor like gene2; Tumor necrosis factor receptor superfamily member 14; Tumor necrosis factor receptor superfamily member 14 precursor; Tumor necrosis factor receptor-like 2

Species

Homo sapiens (Human)

Source

Mammalian cell

Expression Region

39-202aa

Target Protein Sequence

LPSCKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGTYIAHLNGLSKCLQCQMCDPAMGLRASRNCSRTENAVCGCSPGHFCIVQDGDHCAACRAYATSSPGQRVQKGGTESQDTLCQNCPPGTFSPNGTLEECQHQTKCSWLVTKAGAGTSSSHWV
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

48.5 kDa

Protein Length

Partial

Tag Info

C-terminal hFc1-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Lead Time

3-7 business days
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Shelf Life

The shelf life is related to many factors, storage state, storage temperature and the stability of the product itself. Generally, the shelf life of lyophilized form is 6 months at -20°C/-80°C from the date of receipt.

Troubleshooting and FAQs

Protein FAQs

Datasheet & COA

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Images

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
Measured by its binding ability in a functional ELISA. Immobilized TNFRSF14 at 5 μg/ml can bind human TNFSF14(CSB-MP023991HUj2), the EC₅₀ is 49.85-79.31 ng/ml
Activity
Measured by its binding ability in a functional ELISA. Immobilized human TNFRSF14 at 5 μg/ml can bind Biotinylated human TNFSF14 (CSB-MP023991HUj7-B), the EC₅₀ is 1.773-3.707 ng/ml.

Description

TNFRSF14 (HVEM/CD270) functions as a critical immune checkpoint receptor at the crossroads of co-stimulatory and co-inhibitory signaling in tumor microenvironments, making it a high-value target for immuno-oncology drug discovery. This recombinant construct spans the extracellular ligand-binding domain (aa 39–202) with a C-terminal hFc1 tag, produced in mammalian cells to preserve native glycosylation and disulfide-dependent folding essential for accurate ligand recognition. Functional ELISA confirms robust binding to human TNFSF14 (LIGHT) with an EC50 of 49.85–79.31 ng/ml, supporting direct use in receptor-ligand interaction assays, competitive inhibition studies, blocking antibody screening, and affinity characterization by SPR or BLI. Endotoxin levels below 1.0 EU/μg combined with greater than 90% purity satisfy the criteria typical for immune checkpoint research, therapeutic antibody epitope mapping, and small-molecule inhibitor screening campaigns.

Customer Reviews and Q&A

■ Customer Reviews

Average Rating:

5.0 - 1 reviews

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Applications : Binding assay/Protein-protein interaction

Review: We conducted a functional ELISA experiment, and the EC50 was 49.85-79.31 ng/ml. TNFRSF14 showed good binding activity with human TNFSF14. Small inter-batch difference, good repeatability, and relatively stable performance!

By Anonymous

Target Background

Function(From Uniprot)

Receptor 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. Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation. 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. Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response. 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 proinflammatory cytokines. Upon binding to CD160 on activated CD4+ T cells, downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response. May interact in cis (on the same cell) or in trans (on other cells) with BTLA. 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.; (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.

Gene References into Functions

Data suggest that both HVEM and UL144 bind a common epitope of BTLA, whether engaged in trans or in cis; these studies were conducted in cell lines representing B-lymphocytes, T-lymphocytes, and natural killer cells. (HVEM = human herpes virus entry mediator; UL144 = membrane glycoprotein UL144 of Human herpesvirus 5; BTLA = human B- and T-lymphocyte attenuator) PMID:29061848
our data suggested that the BTLA/HVEM pathway contributes to peripheral T cell suppression in hepatocellular carcinoma patients PMID:30116751
TNFRSF14 may serve a tumor suppressive role in bladder cancer by inducing apoptosis and suppressing proliferation, and act as a novel prognostic biomarker for bladder cancer. PMID:30066919
Primary cutaneous follicle center lymphomas with concomitant 1p36 deletion and TNFRSF14 mutations frequently express high levels of EZH2 protein. PMID:29858685
High HVEM Expression is Associated with Cancer Progression in Breast Cancer. PMID:28612127
Report a variant of t(14;18) negative nodal diffuse follicular lymphoma with CD23 expression, 1p36/TNFRSF14 abnormalities, and STAT6 mutations. PMID:26965583
Roles of HVEM are likely to be immunosuppressive rather than activating tumor immunity and it in peripheral blood is a diagnostic marker and therapeutic target for hepatocellular carcinoma. PMID:27987232
Low HVEM expression is associated with pancreatic and ampullary cancer. PMID:28470686
HIV-1 produced from CD4+ T cells bears HSV-2 receptor HVEM and can bind to and enter HSV-2-infected epithelial cells depending on HVEM-gD interaction and the presence of gB/gH/gL. PMID:28809154
Transgenic mice expressing HVEMIg showed a complete resistance to the lethal infection even with 300 MLD50 (survival rate of 100 %). PMID:28671524
HVEM is highly expressed in ovarian serous adenocarcinoma tissues and correlated with the patient clinicopathological features. PMID:28365939
TNFRSF14 and MAP2K1 mutations are the most frequent genetic alterations found in pediatric-type follicular lymphoma (PTFL) and occur independently in most cases, suggesting that both mutations might play an important role in PTFL lymphomagenesis. PMID:28533310
genetic landscape of Pediatric-type follicular lymphoma suggests that TNFRSF14 mutations accompanied by copy-number neutral loss of heterozygosity of the 1p36 locus in over 70% of mutated cases, as additional selection mechanism, might play a key role in the pathogenesis of this disease. PMID:27257180
The increased immune-stimulatory capacity of lymphoma B cells with TNFRSF14 aberrations had clinical relevance, associating with higher incidence of acute GVHD in patients undergoing allogeneic hematopoietic stem cell transplantation. PMID:27103745
These results suggest that TNFRSF14 mutations point towards a diagnosis of follicular lymphomas , and can be used in the sometimes difficult distinction between marginal zone lymphomas and follicular lymphomas PMID:27297871
the overexpression of HVEM in ovarian cancer cells may suppress the proliferation and immune function of T cells, thus leading to the development of ovarian cancer. The current study partially explains the immune escape mechanism of ovarian cancer cells. PMID:27458100
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. PMID:26650888
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. PMID:26202493
HVEM may play a critical role in tumor progression and immune evasion PMID:25750286
Data indicate that tumour-expressing herpes virus entry mediator (HVEMplays a critical role in hepatocellular carcinoma (HCC), suggesting targeting HVEM may be a promising therapeutic strategy for HCC. PMID:25468715
Relative expression of HVEM and LTbetaR modulates canonical NF-kappaB and pro-apoptotic signals stimulated by LIGHT. PMID:24980868
Sequencing of TNFRSF14 located in the minimal region of loss in 1p36.32 showed nine mutations in pediatric follicular lymphoma. PMID:23445872
HVEM plays a critical role in both tumor progression and the evasion of host antitumor immune responses, possibly through direct and indirect mechanisms. PMID:24249528
HVEM gene polymorphisms are associated with sporadic breast cancer in Chinese women. PMID:23976978
The conformation of the N-terminus of herpes simplex virus gD is induced by direct binding to HVEM and nectin-1. PMID:24314649
HVEM functions as a regulator of immune function that activates NK cells via CD160 and limits lymphocyte-induced inflammation via association with B and T lymphocyte attenuator PMID:23761635
BTLA and HVEM may have roles in graft rejection after kidney transplantation PMID:23375291
Studies indicate co-stimulatory and co-inhibitory receptors B7-1, B7-2, CD28 and TNFRSF14 have a pivotal role in T cell biology, as they determine the functional outcome of T cell receptor (TCR) signalling. PMID:23470321
These findings support role for BTLA and/or HVEM as potential, novel diagnostic markers of innate immune response/status and as therapeutic targets of sepsis. PMID:22459947
study described the expression and spatial distribution of HVEM and BTLA in rheumatoid arthritis synovial tissues, and results indicated that HVEM/BTLA may be involved in regulating the progress of joint inflammation PMID:22179929
HVEM-B and T lymphocyte attenuator (BTLA) interactions impair minor histocompatibility antigen (MiHA)-specific T cell functionality, providing a rationale for interfering with BTLA signaling in post-stem cell transplantation. PMID:22634623
Results indicate that mHVEM on leukocytes and sHVEM in sera may contribute to the development and/or progression of gastric cancer. PMID:22113134
These results suggest that the C-terminal portion of the soluble HVEM ectodomain inhibits herpes simplex virus type 1 gD activation and that this effect is neutralized in the full-length form of HVEM in normal infection. PMID:22239829
TNFRSF14 appears to be a serious candidate gene that might contribute to follicular lymphoma development. PMID:21941365
HVEM-BTLA cis complex provides intrinsic regulation in T cells serving as an interference mechanism silencing signals coming from the microenvironment. PMID:21920726
The results of a mutagenesis study of HVEM suggest that the CD160 binding region on HVEM was slightly different from, but overlapped with, the BTLA binding site. PMID:21959263
data show that HVEM stimulatory signals promote experimental colitis driven by innate or adaptive immune cells PMID:21533159
Polymorphisms were associated with MS predisposition, with stronger effect in patients with HHV6 active replication-TNFRSF6B-rs4809330(*)A: P=0.028, OR=1.13; TNFRSF14-rs6684865(*)A: overall P=0.0008, OR=1.2. PMID:20962851
Findings identify TNFRSF14 as a candidate gene associated with a subset of FL, based on frequent occurrence of acquired mutations and their correlation with inferior clinical outcomes. PMID:20884631
We have identified and replicated a novel gene-gene interaction between 2 polymorphisms of TNFRSF members in Spanish patients with RA, based on the hypothesis of shared pathogenic pathways in complex diseases. PMID:20187130
Results provide evidence of an existing relationship between HVEM and obesity, which suggest that this TNF superfamily receptor could be involved in the pathogenesis of obesity and inflammation-related activity. PMID:19680232
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. PMID:11742858
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 PMID:11976496
association of HVEM and nectin-1 with lipid rafts during herpes simplex virus entry PMID:12915568
sHVEM levels were elevated in sera of patients with allergic asthma, atopic dermatitis and rheumatoid arthritis PMID:14749527
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 PMID:15110526
Binding of HVEM to BTLA attenuates T cell activation, identifying HVEM/BTLA as a coinhibitory receptor pair. PMID:15647361
in cells a complex forms through physical associations of HVEM, HSV-1 gD, and at least gH PMID:15767456
distinct herpesviruses target the HVEM-BTLA cosignaling pathway, suggesting the importance of this pathway in regulating T cell activation during host defenses. PMID:16131544
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 PMID:16169851

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Subcellular Location

Cell membrane; Single-pass type I membrane protein.

Tissue Specificity

Widely expressed, with the highest expression in lung, spleen and thymus. Expressed in a subpopulation of B cells and monocytes. Expressed in naive T cells.

Database Links

HGNC: 11912

UNIGENE: Hs.512898

KEGG: hsa:8764

STRING: 9606.ENSP00000347948

OMIM: 602746

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