EEF2 Rabbit IgG antibody Ab Purified
- Known as:
- EEF2 Rabbit Immunoglobulin G (anti-) Antibody Purified
- Catalog number:
- GTX102286
- Product Quantity:
- 0.1 ml
- Category:
- -
- Supplier:
- ACR
- Gene target:
- EEF2 Rabbit IgG antibody Purified
Related genes to: EEF2 Rabbit IgG antibody Ab Purified
- Gene:
- EEF2 NIH gene
- Name:
- eukaryotic translation elongation factor 2
- Previous symbol:
- EF2
- Synonyms:
- EEF-2
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-03-11
- Date modifiied:
- 2015-09-11
Related products to: EEF2 Rabbit IgG antibody Ab Purified
Related articles to: EEF2 Rabbit IgG antibody Ab Purified
- To establish and validate a vitamin-related gene signature for predicting glioma prognosis and immune characteristics, and to explore the functional relevance of EEF2. - Source: PubMed
Publication date: 2026/06/24
Wu LiqinLu JunfeiZhang QingHuang TaoChen YanfangShi HaojunCai Jun - To investigate the differences in molecular responses between the gills and hepatopancreas of freshwater-cultured Litopenaeus vannamei under chronic nitrite stress, a 30-day chronic stress experiment was conducted with a control group and a stress group. Transcriptomic analysis of the gills and hepatopancreas was performed using Illumina sequencing; differentially expressed genes (DEGs) were identified, and GO, KEGG, GSEA, PPI, and RT-qPCR validation were carried out. The results showed that 196 DEGs (161 up-regulated and 35 down-regulated) were identified in the gills, and 287 DEGs (199 up-regulated and 88 down-regulated) in the hepatopancreas, with only 18 DEGs shared between the two tissues. DEGs in the gills were enriched in oxidoreductase activity, glycerophospholipid metabolism, and tyrosine metabolism; DEGs in the hepatopancreas were enriched in lipid transporter activity, phagosome, ECM-receptor interaction, and riboflavin metabolism. GSEA revealed significant suppression of the mTOR pathway in the gills and the Polycomb complex pathway in the hepatopancreas. PPI network analysis identified hub genes P5CS and eEF2 in the gills, and PER, TUBB1, SHMT, and TUBB4B in the hepatopancreas. RT-qPCR validation was consistent with the RNA-seq results (R = 0.764). This study indicates that, under chronic nitrite stress, the gill response is centered on redox regulation and inhibition of growth metabolism, whereas the hepatopancreas response primarily involves lipid transport, cytoskeletal remodeling, and phagosome activation. The two tissues synergistically adapt through fundamental biosynthetic and motor protein pathways. This research provides molecular evidence for deciphering the nitrite tolerance mechanisms in freshwater-cultured shrimp. - Source: PubMed
Publication date: 2026/06/22
Li XinxinLi XuenanDai Xilin - Periodontitis, a common chronic inflammatory disease, causes connective tissue degradation, alveolar bone resorption, and tooth loss. G protein coupled receptor class C group 5 member A (GPRC5A) regulates chronic inflammation in several diseases, but its role in periodontitis remains unclear. This study investigated GPRC5A expression and function in periodontitis. In human tissues, GPRC5A expression was assessed by immunohistochemistry and quantitative real-time PCR (qRT-PCR). In vivo, adeno associated virus (AAV) mediated GPRC5A silencing was applied in a murine periodontitis model. In vitro, mechanistic studies used small interfering RNA (siRNA) knockdown, co-immunoprecipitation (Co-IP), mass spectrometry, and western blot in periodontal ligament cells (PDLCs). GPRC5A was upregulated in inflamed periodontal tissues, and its downregulation reduced alveolar bone loss and periodontitis severity in mice. GPRC5A knockdown suppressed inflammatory cytokine production and NF-κB activation in lipopolysaccharide (LPS) stimulated PDLCs. β-arrestin 2 (ARRB2) expression paralleled GPRC5A changes, and mass spectrometry/Co-IP identified eukaryotic elongation factor 2 (EEF2) as an ARRB2 binding partner. GPRC5A silencing reduced LPS induced ARRB2 expression and EEF2 phosphorylation. These data suggest a possible mechanistic link that GPRC5A downregulation mitigates periodontitis through the ARRB2‑EEF2 pathway, though direct evidence of causality is still needed. - Source: PubMed
Publication date: 2026/06/11
Hu YuhanLiu RunxuanChen XinxiaoShang Lingling - Translation is accompanied by the rotation of the small and large ribosomal subunits relative to each other. Here, we use single-molecule Förster resonance energy transfer between fluorophores introduced into ribosomal proteins uS15 and eL30 to follow the intersubunit dynamics of Saccharomyces cerevisiae ribosomes. Similar to their bacterial counterparts, yeast ribosomes are observed to sample two predominant FRET states corresponding to the nonrotated (NR) and rotated (R) conformations. Our data yield further evidence that intersubunit rotation is coupled to tRNA transitions between the classical and hybrid binding states. The elongation cycle, which comprises tRNA binding, peptide transfer, and mRNA-tRNA translocation, is accompanied by switching from NR to R, and then back to the NR conformation. We find that fungal elongation factor 3 (eEF3) stabilizes the NR conformation of the ribosome. Our data are consistent with the model suggesting that eEF3 facilitates E-site tRNA release at the late step of mRNA-tRNA translocation, following the reverse intersubunit rotation induced by the universally conserved elongation factor 2 (eEF2). Our uS15-eL30 smFRET assay provides the basis for investigating eukaryotic mechanisms of translation regulation, including ribosome pausing, stalling, and frameshifting. - Source: PubMed
Das AnanyaGrove Amy KIvanov Aleksandr VWakabayashi HironaoErmolenko Dmitri N - Newcastle disease (ND) caused by Newcastle disease virus (NDV) infection is a highly contagious avian disease that causes substantial threat to the global poultry industry. Emodin (EMO), a member of the free anthraquinone compounds derived from traditional Chinese medicines, is known for its antibacterial, antiviral, antitumor, and antioxidant activity. However, the anti-NDV activity and potential mechanism of action of EMO remains unknown. In this study, EMO was found to exert a remarkable anti-NDV activity in a dose- and phase-dependent manner. In addition, EMO restricted NDV replication mainly by affecting the production of viral proteins, but not by inhibiting the viral RNA synthesis and transcription. Moreover, the EMO treatment-induced reduction of viral proteins was correlated well with the increased phosphorylation level of eukaryotic elongation factor 2 (eEF2) in NDV-infected cells, which was further confirmed by inhibition of eEF2 kinase (eEF2K) activity with pharmacological inhibitors NH125 and A-484954, respectively. Meanwhile, multiple signaling cascades, including p38 MAPK, mTORC1/p70 S6K, and ERK1/2/p90 RSK1, were found to regulate the phosphorylation levels and activities of eEF2K and eEF2 by which EMO reduced viral protein production and inhibited NDV replication. Furthermore, molecular docking combined with protein-protein interaction analysis showed that EMO could form stable hydrogen bond structures with the NDV N protein at the Lys32 and Leu225 residues, and attenuate its interaction with eIF4E to decrease the production of viral proteins. These findings reveal the anti-NDV effect and the underlying mechanism of EMO, offering a potential natural compound for the development of antiviral strategies against NDV. - Source: PubMed
Publication date: 2026/05/25
Wu WenjieXia RongjingMa SiHu ZengleiDuan Zhiqiang