IFNGR2 _ IFNGT1 antigen
- Known as:
- IFNGR2 _ IFNGT1 antigenic
- Catalog number:
- 'H00003460-Q01-25
- Product Quantity:
- 25
- Category:
- -
- Supplier:
- ACR
- Gene target:
- IFNGR2 _ IFNGT1 antigen
Related genes to: IFNGR2 _ IFNGT1 antigen
- Gene:
- IFNGR2 NIH gene
- Name:
- interferon gamma receptor 2
- Previous symbol:
- IFNGT1
- Synonyms:
- AF-1
- Chromosome:
- 21q22.11
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: IFNGR2 _ IFNGT1 antigen
'F 4_80 Antigen (mouse) Host Rat'F 4_80 Antigen (mouse) Host Rat(Anti_Tg)Thyroglobulin Antigen(Des-Asp187)-Melanocyte Protein PMEL 17 (185-193) (human, bovine, mouse)
(Des-Asp187)-ME20M_ME20S (185-193) (human, bovine, mouse), (Des-Asp187)-Melanocyte Lineage-Specific Antigen GP100 (185-193) (hu(Des-Asp187,Met186)-Melanocyte Protein PMEL 17 (185-193) (human, bovine, mouse)
(Des-Asp187,Met186)-Melanoma-Associated ME20 Antigen (185-193) (human, bovine, mouse), (Des-Asp187,Met186)-95 kDa Melano(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Draxin) C1ORf187, Antigen blocking peptide(Val438)-Tyrosinase (432-444) (human)
(Val438)-LB24-AB (432-444) (human), (Val438)-Monophenol Monooxygenase (432-444) (human), (Val438)-SK29-AB (432-444) (human), (Val438)-Tumor Rejection Antigen AB (0x19 Antigen0x2 Antigen1,25-dihydroxyvitamin D3 Competitive ELISA, Coated with Antigen105 kDa islet cell antigen,BEM-3,Brain-enriched membrane-associated protein tyrosine phosphatase,ICA105,PTP IA-2,PTPLP,Ptprn,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase-like N,R-P Related articles to: IFNGR2 _ IFNGT1 antigen
- Diabetic kidney disease (DKD) is a major microvascular complication of diabetes, with microcirculatory dysfunction and immune injury as its core pathological features. Extracellular vesicles (EVs) act as key mediators of intercellular communication, but it remains unclear whether EV-encapsulated microRNAs (miRNAs) are involved in the crosstalk between endothelial cells (ECs) and monocytes in DKD. - Source: PubMed
Publication date: 2026/06/10
Jing JiaxingAn JiashengChen XiangmeiCong BinYu WentaoGao Weijuan - Interferon-gamma (IFN-γ) serves as an inflammatory cytokine essential for modulating innate and cell-mediated immune responses by associating with a receptor complex composed of IFNGR1 and IFNGR2. In this research, the entire cDNA of IFNGR2 from Nibea albiflora was cloned and functionally analyzed (referred to as NaIFNGR2), with the complete cDNA sequence measuring 924 bp and encoding 307 amino acids. The phylogenetic analysis and multiple sequence alignment revealed a significant similarity of NaIFNGR2 with homologous sequences found in other bony fish, especially within the FNⅢ domain and the transmembrane region. Real-time PCR analysis revealed that NaIFNGR2 was consistently expressed across all examined tissues, including the head-kidney, spleen, liver, kidney, gill, muscle, and blood, with the highest levels found in the gills. Following stimulation with Polyinosinic-polycytidylic acid (Poly (I:C)), Vibrio alginolyticus, or Vibrio parahaemolyticus, the mRNA levels of NaIFNGR2 showed an increase in a time-dependent manner. Subcellular localization studies indicated that NaIFNGR2 resided on the cell membrane and NaIFN-γ, once synthesized within the cell, was transported to the membrane to interact with NaIFNGR2. Additionally, NaIFNGR1 and NaIFNGR2 were completely co-localized on the cell membrane, which was consistent with the findings that NaIFNGR1 and NaIFNGR2 could form a heterodimeric complex. Being treated with the NaIFN-γ recombinant protein, both alone and in combination with LPS, various concentrations of NaIFN-γ were non-toxic to the growth of RAW 264.7 macrophages and significantly promoted their proliferation. The expression levels of IL-1β, IL-6, and TNF-α proteins were markedly upregulated in a concentration- and time-dependent manner following 24 and 48 h of combined stimulation. Furthermore, the secretion of nitric oxide (NO) was significantly increased after 36 and 48 h of stimulation, highlighting the regulatory effect of NaIFN-γ on macrophages and its influence on the inflammatory response. Collectively, the findings indicated that the NaIFN-γ ligand-receptor system was present in N. albiflora and played a crucial role in the immune response to pathogenic bacterial infections, enhancing our comprehension of the function of IFN-γ within the immunomodulatory processes of teleosts. - Source: PubMed
Publication date: 2026/04/27
Yuan HanbingLiu YongxinZhou XuXu DongdongChi ChangfengLü ZhenmingLiu Huihui - This study aimed to investigate the regulatory role of circular RNAs (circRNAs) in lupus nephritis (LN) and to explore their potential mechanisms. - Source: PubMed
Publication date: 2026/04/24
Gong SiwenWang ChongyaoEmiliia GainetdinovaFu YutingDing XiaotongHe WenyaZhang LeiLiu RuichanWang XingzhiBao YushiSui Manshu - Transient receptor potential (TRP) channels regulate Ca homeostasis and tumor malignant phenotypes, whereas their prognostic relevance and therapeutic implications in glioblastoma (GBM) remain poorly characterized. - Source: PubMed
Publication date: 2026/04/19
Sun RunfengZhu LongLu ZhichaoWang ZihengFeng SuyinZhao Jingwei - Immune checkpoint blockade (ICB) is a standard treatment for several types of human cancer, yet we still lack a deep understanding of the mechanisms underlying primary resistance. Tumor-intrinsic defects in immune recognition and interferon-gamma (IFNγ) signaling pathways facilitate immune evasion and may limit the efficacy of ICB. Here, we delineate the mutational landscape and functional consequences of amino acid substitutions in key immune-related genes, B2M, CALR, IFNGR1, IFNGR2, JAK1, and JAK2, across more than 12,000 primary tumors and cancer cell lines. Genomic alterations affecting the coding regions of at least one of these genes were identified in approximately 11% of cancers, with missense variants accounting for 55% of these events. B2M, encoding the invariant light chain of the heavy chain-I (HLA-I) complex, exhibited the highest mutation frequency per base pair, the mutations predominantly involving truncating variants. A curated set of 2156 missense mutations in B2M and in components of the IFNγ-signaling pathway (IFNGR1, IFNGR2, and JAK2) was analyzed using SIFT, PolyPhen-2, and AlphaMissense, yielding predicted pathogenicity rates of 52%, 35%, and 27%, respectively. The functional assays, performed in lung cancer cells, revealed JAK2 and IFNGR1 variants that impaired IFNγ-mediated transcriptional activation and growth suppression, and B2M variants that disrupted HLA class I complex formation. Notably, AlphaMissense predictions showed the highest concordance with experimental data. These findings provide a detailed mutational map of antigen presentation and IFNγ-response components in cancer. Overall, our results provide a resource of specific mutations in genes involved in immune pathways that compromise tumor immunogenicity and will serve for support in patient selection for response to ICB. - Source: PubMed
Publication date: 2026/04/04
Diaz Cristina AMorillas Juan MNavajas-Chocarro PabloProvenzano ValentinaSetien FernandoEsteller ManelSanchez-Cespedes Montse