Polyclonal Rabbit NEDD8 Antibody
- Known as:
- Polyclonal Rabbit NEDD8 Antibody
- Catalog number:
- abx000774
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- Polyclonal Rabbit NEDD8 Antibody
Related genes to: Polyclonal Rabbit NEDD8 Antibody
- 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: Polyclonal Rabbit NEDD8 Antibody
Related articles to: Polyclonal Rabbit NEDD8 Antibody
- Ubiquitin and ubiquitin-like proteins (UBLs) have emerged as critical regulators of protein homeostasis and cellular signaling, processes that are increasingly recognized as central to the pathogenesis of Alzheimer's disease (AD). This review explores the expanding roles of UBL modifiers, including SUMO, NEDD8, ISG15, UFM1, and ATG8/ATG12, in the development and progression of AD. We discuss how these post-translational modifications influence key pathological features of AD such as amyloid-beta accumulation and neurofibrillary tangles formation, as well as their impact on neuronal function, proteostasis, and neuroinflammation. Recent advances in our understanding of the enzymatic machinery mediating these modifications, and the interplay between different UBL proteins, offer new insights into the molecular mechanisms underlying AD. Furthermore, we highlight emerging therapeutic strategies targeting UBL pathways, which may provide novel avenues for intervention in AD. By integrating current findings, this review underscores the significance of UBL proteins in AD and identifies future directions for research aimed at unraveling their complex roles in neurodegeneration. - Source: PubMed
Publication date: 2026/05/08
Yan TingxiangVaquer JustineSpringer WolfdieterFiesel Fabienne C - 5-Methylcytosine (m5C) is an important RNA methylation modification implicated in tumor initiation and progression through its effects on RNA transcription, structural conformation, and stability. However, the role of the interaction between circular RNAs (circRNAs) and m5C modification in oncogenesis remains limited. This study aimed to elucidate the molecular mechanism by which m5C-modified circCEP70 facilitates radioresistance in rectal cancer (RC). - Source: PubMed
Publication date: 2026/05/07
Hu YouShan ZhiliSun XueLiang JinmingWang LeiZhou XiaojunChen Xin - Plant Cullin RING Ubiquitin E3 ligases (CRLs) play a critical role in targeted protein degradation, essential for physiological development and stress adaptation. The deneddylase activity of the COP9 signalosome (CSN) tightly regulates the cellular balance of neddylated cullins, which is crucial for maintaining the full spectrum of CRL functions. Although selective inositol polyphosphates (InsPs) act as cofactors in plant responses that involve ubiquitylation of negative regulators, their connection to CSN-CRL activities has remained unclear. In this study, we reveal that the two Arabidopsis thaliana InsP-kinases, IPK1 and ITPK1, physically interact and orchestrate the metabolic regulation of the CSN holo-complex activity. Notably, ITPK1 deficiency lowers Nedd8 processing rates, elevates the cellular ratios of neddylated cullins, and disturbs the dissociation equilibrium of CSN5 and CUL1 from the holo-complex. These findings uncover a novel autoregulatory switch in CSN functions, governed by deneddylation activity. Furthermore, we demonstrate that the phosphate starvation response (PSR), induced in phosphate-limited wild-type plants and constitutively active in the InsP-kinase mutants, is partly regulated by reduced deneddylation rates, which affect the stability of SPX4, a key negative regulator of PSR. Pharmacological inhibition of cullin neddylation stabilizes SPX4 and impairs PSR, thereby linking CSN-CRL dynamics to phosphate sensing. Conversely, pharmacologically inhibiting CSN5 deneddylase activity causes wild-type plants to exhibit PSR phenotypes similar to those of the InsP-kinase mutants. Collectively, these results reveal that specific InsP-kinases are partly involved in modulating plant PSR by fine-tuning the coordination between CRL and CSN activities. - Source: PubMed
Publication date: 2026/05/05
Walia YashikaNoopur MedhaBhattacharya IshanaSahoo Bhaskar ChandraKasera MritunjayPullagurla Naga JyothiDutta SmritikanaLiu GuizhenSchaaf GabrielJessen HenningLaha DebabrataBhattacharjee SouvikBhattacharjee Saikat - As the core scaffold protein of the Cullin-RING ligase 5 (CRL5) complex, CUL5 regulates the stability of multiple substrate proteins through the ubiquitin-proteasome system (UPS), playing a crucial role in the initiation, progression, and cellular therapy of malignant tumors. This review systematically elaborates the context-dependent role, molecular regulatory network, and therapeutic targeting potential of CUL5-mediated ubiquitination in cancer cell therapy. The activity of CUL5 is highly dependent on NEDD8-mediated neddylation, and its dysregulation indirectly influences tumor cell proliferation, apoptosis, metabolic reprogramming, angiogenesis, and the immune microenvironment by modulating key signaling pathways such as NOXA, mTORC, TRAF6/NF-κB, and JAK/STAT. Notably, CUL5 exhibits dual regulatory functions in various cancers, and its expression level correlates differently with prognosis depending on tumor type. In recent years, the development of inhibitors and nano-delivery systems targeting CUL5 and its related pathways has provided novel strategies for precisely targeting CUL5. Moreover, in adoptive cell therapies (e.g., CAR-T, TCR-T, CAR-NK), modulation of CUL5 expression can significantly enhance immune-cell proliferation, cytokine secretion, and anti-tumor efficacy. This article summarizes the multidimensional role of CUL5 in tumor cell therapy and prospects its potential as a novel therapeutic target in combined therapies and precision medicine. - Source: PubMed
Publication date: 2026/04/17
Lu YuanchenQian YichenMa YueShao XianhuaXie Jianjun - Colorectal cancer (CRC) is the second leading cause of cancer-related deaths worldwide, and one of the best-characterized drivers is oncogenic Wnt signaling. In this study, we demonstrated that Orlistat, an FDA-approved anti-obesity drug, is a unique inhibitor of oncogenic Wnt signaling and CRC. We confirmed that the known target FASN was not associated with Orlistat inhibition of CRC, and identified the NEDD8-conjugating enzyme UBC12 (UBE2M) as a candidate target instead. The direct engagement of Orlistat and UBC12 was confirmed by ITC assay with a KD value of 678 nM. Of note, Orlistat inhibited the NEDD8-conjugating activity of UBC12 and blocked UBC12 interaction with DCN1 (defective in cullin neddylation 1), thereby selectively suppressing Cullin 1 neddylation. In addition, overexpression of UBC12 positively regulated Wnt/β-catenin signaling in normal cells, while depletion of UBC12 not only inhibited oncogenic Wnt signaling but also abrogated Orlistat's inhibition of Wnt signaling and cell proliferation in CRC cells. Taken together, our findings revealed UBC12 as a novel Orlistat target, and identified UBC12 as a potential therapeutic target for Wnt-dependent cancers. - Source: PubMed
Publication date: 2026/04/30
Shen MengzhenLi HuihuiXuan YingZhu HongyanChen LizheHao PiliangZhang ChengqianFang JiansongZhou XianglianYan RongQu YiKe Xisong