Human Polyclonal NEDD8 Ab
- Known as:
- Human Polyclonal NEDD8 Antibody
- Catalog number:
- a0591
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- ABclonal
- Gene target:
- Human Polyclonal NEDD8
Ask about this productRelated genes to: Human Polyclonal NEDD8 Ab
- Gene:
- NEDD8 NIH gene
- Name:
- NEDD8 ubiquitin like modifier
- Previous symbol:
- -
- Synonyms:
- Nedd-8
- Chromosome:
- 14q12
- Locus Type:
- gene with protein product
- Date approved:
- 1994-01-21
- Date modifiied:
- 2019-04-04
Related products to: Human Polyclonal NEDD8 Ab
Related articles to: Human Polyclonal NEDD8 Ab
- Keratoconus (KC) is an adolescent-onset vision-impairing corneal disorder with incompletely elucidated pathogenesis. This study aims to elucidate the regulatory role of NEDD8 in the Hippo-YAP signaling pathway and its influence on the corneal pathology, thereby providing a theoretical basis for mechanistic studies and targeted therapy of KC. - Source: PubMed
Qu JunpengZhang XiaowenWei ChaoYu HuiminDou ShengqianGao Hua - Protein neddylation modification involves transfer of neural precursor cell expressed developmentally downregulated protein 8 (NEDD8), a ubiquitin-like protein, to substrates through a three-step enzymatic cascade mediated by NEDD8-activating enzyme (NAE), conjugating enzyme and ligases. Given Cullin-RING ligases (CRLs) as the uppermost substrates which regulate degradation of numerous proteins, neddylation modulates numerous biological functions, including tumor development. MLN4924, a potent NAE inhibitor, has emerged as a promising anti-cancer agent based on neddylation interference. However, resistance to MLN4924 poses a significant challenge. Growing evidence suggests that neddylation directly and indirectly modulates the tumor immune microenvironment (TIME), providing novel insights into its impact on tumor dynamics and the development of resistance to MLN4924. This understanding indicates that targeting neddylation could potentially be combined with immunotherapies for more effective treatment strategies. Here, we briefly outline how neddylation is organized and its modulatory roles in both tumor cells and intertumoral immune cells, proposing an optimistic outlook for neddylation-targeted therapy. - Source: PubMed
Publication date: 2026/02/06
Xu MengnaLiu WeixiaoLiu FanXie Ping - A detailed study of the structure-activity relationship (SAR) in a series of phenyl dihydrouracil (PDHU) derivatives as promising chemotypes for protein degrader discovery is reported. Evaluation of cereblon binding for several dozen PDHU-derived building blocks showed that over 20 compounds with various substituents at the phenyl ring showed over 50% displacement of labeled thalidomide at 10 μM. Most potent representatives bearing methyl substituents were used to synthesize 72 PROTACs by conjugating with JQ1 through a series of linear linkers with or without additional heteroatoms. A series of assays (including binary and ternary complex formation, as well as cell-based BRD4 degradation) allowed the establishment of SAR trends related to the linker nature and length. Compounds with (CH), (CH), and especially (CH) linkers demonstrated the best results in both BRD4 degradation (DC = 16-52 nM) and cell viability assays, outperforming dBET1, a well-known thalidomide-based protein degrader, in the HepG2 cell line. Mechanistic experiments performed in the presence of a proteasome inhibitor, a NEDD8-activating enzyme inhibitor, and excess of cereblon or BRD4 ligands, as well as Western blot assays, confirmed that BRD4 degradation is indeed involved in the compound's cellular effects. The most potent representatives (2/5-Me-PDHU11) can be promising tools for biomedical research. - Source: PubMed
Publication date: 2026/05/07
Shyshlyk OlehStadnichenko VladyslavDiachenko OleksandrChernysh IrynaBeshtynarska AnnaAlieksieieva DianaKhotinets DianaOleksiak OleksiiLesyk DmytroYeremenko YelyzavetaBiitseva Angelina VBorysko PetroYarmolchuk VolodymyrTolstanova Ganna MGrygorenko Oleksandr O - The organized chromatin configuration in meiosis prophase I is crucial for spermatogenesis and male fertility, involving a series of tightly coordinated events mediated by numerous proteins. Neddylation, a ubiquitin-like post-translational modification, conjugates NEDD8 to substrate proteins and thus regulates protein degradation via activating Cullin-RING E3 ligases. Despite its importance in other cellular processes, its role in meiosis remains elusive. - Source: PubMed
Publication date: 2026/05/29
Tang NingyuanGuo QinghuaZhao WenzhenWang LiFu RongXin ZhixiangZhang ZongqinLiu Yue - The Neddylation pathway is excessively activated in the occurrence and development of various cancers. However, there is currently a lack of comprehensive analysis of the Neddylation pathway in hepatocellular carcinoma (HCC). We treated HCC cells with a Neddylation pathway inhibitor (MLN4924) to observe its effects on the biological functions of HCC cells. Additionally, we constructed a Neddylation-related risk score (NRS) in HCC. Subsequently, we assessed the clinical value of NRS in predicting the prognosis of HCC and the efficacy of immunotherapy. Finally, we investigated the role of Proteasome 26S Subunit, Non-ATPase 1 (PSMD1) in the malignant progression of HCC through in vivo and in vitro experiments. MLN4924 significantly inhibits the proliferation and migratory capacity of HCC cells, promotes apoptosis, and upregulates PD-L1 expression. Moreover, we have confirmed through in vivo and in vitro experiments that MLN4924 can enhance the sensitivity to Sorafenib. Additionally, we found that patients in the high NRS group have poor prognoses and are prone to developing resistance to treatments such as Sorafenib and Oxaliplatin, while being more sensitive to 5-Fluorouracil and immunotherapy. Finally, in both in vitro and in vivo experiments, it was found that knocking down PSMD1 can weaken the proliferation and metastatic capacity of HCC cells. Furthermore, knocking down PSMD1 can inhibit the levels of PD-L1 protein and NEDD8 protein that binds to Cullin in HCC cells. Mechanistically, we found that PSMD1 stabilizes the protein expression of β-catenin by inhibiting its degradation through the ubiquitin-proteasome system, thereby influencing the expression of PD-L1. In conclusion, this study reveals that Neddylation-related characteristics can effectively predict the prognosis and immunotherapy outcomes of HCC. Furthermore, targeting PSMD1 may represent a potential therapeutic approach for HCC. - Source: PubMed
Publication date: 2026/05/24
Liu ZitaoZuo ChengWu ChangleiTian HuakaiZhu ZhengmingZhu WenjieSun Liang