Mouse Anti-Human CD160, FITC-labeled
- Known as:
- Mouse Antibody toHuman CD160, fluorecein-labeled
- Catalog number:
- 129-10106
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Ray Biotech
- Gene target:
- Mouse Anti-Human CD160 FITC-labeled
Related genes to: Mouse Anti-Human CD160, FITC-labeled
- Gene:
- CD160 NIH gene
- Name:
- CD160 molecule
- Previous symbol:
- -
- Synonyms:
- BY55, NK1, NK28
- Chromosome:
- 1q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-02
- Date modifiied:
- 2016-10-05
Related products to: Mouse Anti-Human CD160, FITC-labeled
Related articles to: Mouse Anti-Human CD160, FITC-labeled
- Somatic mutations can rewire tumor-immune interactions to favor cancer progression. Here, we define the functional impact of missense mutations in Herpesvirus entry mediator (HVEM, TNFRSF14), a receptor frequently altered in lymphoma and melanoma. - Source: PubMed
Publication date: 2026/09/11
Lin Wai WaiHuang SarahBalmert OliviaBjordahl RyanWare Brian CMoshayedi ArefNguyen JenniferWare Carl FŠedý John R - Herpes simplex virus 1 (HSV‑1) establishes infection through coordinated interactions of multiple viral glycoproteins with host cell receptors. Interactions between the viral glycoprotein D (gD) and the immunomodulatory cellular receptor HVEM (herpesvirus entry mediator) critically influence HSV‑1 latency and reactivation by regulating both receptor engagement and immunomodulatory signaling in the corneal epithelium, immune cells, and neurons. The underlying mechanisms of these phenotypes remain poorly understood because no tools selectively block their interaction. To dissect the contributions of individual amino acids (aa) to HVEM binding, we co‑immunoprecipitated wild‑type (WT) and mutant (Q27P and Q27A‑L28A‑T29A) forms of gD that disrupt gD binding to HVEM. We found that gD aa Q27-T29 were critical for HVEM binding, with the triple mutant showing greater disruption of HVEM binding than the Q27P single mutation, as assessed by co-immunoprecipitation and immunostaining. To map gD binding to HVEM and assess functional relevance, we constructed two recombinant viruses: a single-amino-acid (aa) gD mutation (v27 virus) and a triple-aa mutation in gD (v27-29 virus). Replication of both mutant viruses was comparable to that of the WT virus in four mammalian cell lines, except in Neuro2a cells. However, using confocal microscopy, HVEM protein expression was reduced in v27-29-infected Neuro2a cells, with no gD colocalization observed. Although Neuro2a cells infected with the single gD v27 mutant also showed less HVEM-gD colocalization than Neuro2a cells infected with WT virus, gD protein levels were not affected. RT‑PCR analysis of Neuro2a cells infected with single and triple gD mutants showed significantly less expression of viral glycoproteins (gB, gC, gD), host receptors (HVEM, nectin‑1, 3‑O‑sulfated heparan sulfate), and HVEM ligands (BTLA, LIGHT, Ltα, CD160), with the most pronounced effects observed for the triple v27‑29 mutant virus. Together, these results show that aa Q27-T29, rather than aa Q27 alone, are essential to completely block gD binding to HVEM and, consequently, affect overall receptor homeostasis. - Source: PubMed
Publication date: 2026/09/08
Arya DeepakTormanen KatiOh Jay JWang ShaohuiGhiasi Homayon - Immune checkpoint inhibitors (ICIs) have improved outcomes for patients with melanoma and are now the standard of care for high-risk and advanced disease. However, long-term benefits are observed in only around 25% of patients, with significant risk for immune-related adverse events, highlighting the need for predictive biomarkers. To develop a minimally invasive, pre-treatment biomarker strategy, we profiled functional and subset-specific transcripts in peripheral blood T lymphocytes (PBTLs) and applied machine learning to identify predictive signatures. Patients were enrolled prior to receiving ICI monotherapy in the adjuvant (Exploratory n=61, Validation=78) or metastatic (Exploratory n=48, Validation=46) settings. Following feature selection, random forest models were trained and benchmarked against empirical null models. In the adjuvant setting, CD160 and GZMB predicted recurrence (95th percentile), while treatment-limiting toxicity was predicted by a signature comprising TNFRSF18, VTCN1, TIGIT, CCR4, and AHR (97th percentile). In the metastatic setting, baseline CD45RB, a marker of T-cell differentiation, most strongly predicted progression within one year (93.9th percentile). Distinct signatures in the adjuvant and metastatic settings suggest differences in T-cell programs associated with patient outcomes. These findings support further evaluation of pre-treatment circulating T-cell transcriptional profiles as predictors of ICI response and toxicity in melanoma. - Source: PubMed
Publication date: 2026/08/25
Lepola NoahDravillas CarolineGray ShannonBodnar Michael SArya NamrataWu RichardVerschraegen ClaireCarson William EKendra Kari LSpakowicz Daniel JBurd Christin E - Regulatory T cells (Treg) play a central role in maintaining immune homeostasis, and the implementation of in vitro induced Treg cells (iTreg) to control immune function has significant potential in clinical medicine. The clinical application of iTreg has been limited by their poor stability. To better define the molecular characteristics of human iTreg, we performed a data-independent acquisition proteomics, detecting over 8000 proteins and providing a quantitative comparison of their relative levels in iTreg and activated Th0 cells. Consistent with the known molecular characteristics of Treg, several Treg signature proteins, including FOXP3, IKZF4, IL2RA, CTLA4, PD-1, IKZF3, LAG3, RUNX1 and hypermethylated in cancer 1, were identified and validated using Tier two targeted SRM and/or qRT-PCR. Notably, Leupaxin level was upregulated during Treg cell differentiation. Functional studies demonstrated that LPXN-deficient cells showed impaired expression of Treg protein markers FOXP3, IKZF4 and IKZF3 and impaired suppression of effector T cells. In addition, we identified a distinct CD160 iTreg subpopulation characterized by a distinct proteomic signature as compared to CD160 iTreg. Together, these findings provide a high-resolution proteomic landscape of human iTreg and identified a novel role of LPXN in the development and suppressive activity of iTreg. - Source: PubMed
Publication date: 2026/08/20
Batkulwar KedarAndrabi Syed Bilal AhmadKattelus RoosaBuchacher TanjaArnkil IlonaStarskaia InnaRasool OmidMoulder RobertLahesmaa Riitta - Epstein-Barr virus-associated hemophagocytic lymphohistiocytosis (EBV-HLH) is a life-threatening hyperinflammatory syndrome paradoxically characterized by excessive cytokine production and immune activation despite failure to clear Epstein-Barr virus (EBV). The cellular mechanisms underlying immune dysregulation in EBV-HLH remain incompletely understood. - Source: PubMed
Publication date: 2026/08/05
Luo XiaodanChen AoLiu JianboShi BoyunTang JianliHuang JiayuYuan DanyunLiang ZhimingTan HuoZheng Runhui