KAT5 pSer90 antibody Ab
- Known as:
- KAT5 pSer90 (anti-) Antibody
- Catalog number:
- 1488286
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Acris antibodies
- Gene target:
- KAT5 pSer90 antibody
Related genes to: KAT5 pSer90 antibody Ab
- Gene:
- KAT5 NIH gene
- Name:
- lysine acetyltransferase 5
- Previous symbol:
- HTATIP
- Synonyms:
- TIP60, PLIP, cPLA2, HTATIP1, ESA1, ZC2HC5
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-04-13
- Date modifiied:
- 2016-10-05
Related products to: KAT5 pSer90 antibody Ab
Related articles to: KAT5 pSer90 antibody Ab
- Lysine acetyltransferase 5 (KAT5) plays a critical role in epigenetic regulation and is closely associated with the progression of various cancers, particularly hepatocellular carcinoma. However, convenient and portable methods for monitoring KAT5 activity remain limited. Herein, we report a coordination-regulated colorimetric sensing platform based on the localized surface plasmon resonance of gold nanoparticles (AuNPs) for KAT5 activity detection. In this strategy, Zn coordinates with ethylenediamine (en) to form Zn(en) complexes, which induce AuNPs aggregation and a distinct plasmonic color change. In the presence of coenzyme A (CoA), generated during the KAT5-catalyzed acetylation reaction, Zn preferentially binds to thiol-containing CoA, suppressing Zn(en) formation and inhibiting AuNPs aggregation. As a result, KAT5 activity is indirectly converted into a measurable colorimetric signal with a detection limit of 1.9 pg/mL (3σ/slope). To enable portable analysis, smartphone-based image processing was integrated, using the blue-to-red (B/R) ratio for quantification. The platform was further applied to investigate histone acetylation in cancer cells and circulating tumor cell (CTCs)-like models during epithelial-mesenchymal transition, revealing dynamic changes in KAT5 activity. This coordination-mediated AuNPs strategy provides a simple and portable tool for monitoring cancer-related enzymatic activity, with potential applications in liquid biopsy, early cancer diagnosis, and precision medicine. - Source: PubMed
Publication date: 2026/05/28
Zhao XingyuCheng CaizhaoChen JiayunYao JingluZhang QingqingHu YufangQing Zhihe - Anaplastic thyroid carcinoma (ATC) is an exceptionally aggressive malignancy with dismal survival, largely due to intrinsic cisplatin resistance. This study identifies a novel mechanism by which small extracellular vesicles (sEVs) promote chemoresistance by enhancing DNA repair via protein lactylation. ATC cells secrete sEVs enriched with Annexin A2 (ANXA2). Upon delivery to recipient ATC cells, ANXA2 stabilizes the interaction between SRC kinase and lactate dehydrogenase A (LDHA), leading to increased LDHA phosphorylation (Y10), enzyme activity, and lactate production. The resulting lactate surge serves as a substrate for lysine lactylation. Ku80 (XRCC5) is identified as a key lactylation target at K265, catalyzed by the acyltransferase KAT5. This lactylation modification strengthens the interaction between Ku80 and its partner Ku70 (XRCC6), stabilizing the initial DNA-end binding complex in the non-homologous end-joining (NHEJ) repair pathway. Consequently, NHEJ efficiency is significantly enhanced, enabling ATC cells to rapidly repair cisplatin-induced DNA double-strand breaks and survive treatment. Genetic disruption of the XRCC5-K265 lactylation site or pharmacological inhibition of LDHA sensitizes ATC xenograft tumors to cisplatin, while in vitro, inhibition of the SRC/LDHA axis produces a similar chemosensitizing effect. This work unveils the ANXA2 sEV/SRC/LDHA/lactate/XRCC5-lactylation axis as a critical driver of NHEJ-mediated chemoresistance in ATC, offering new potential therapeutic targets. - Source: PubMed
Publication date: 2026/07/03
Su ShanshanXiong YiShanLiang YuxuanMin XiangDai Daofeng - Pulmonary fibrosis (PF) remains a lethal progressive disease with poorly defined molecular drivers. Epithelial dysfunction and metabolic reprogramming contribute to PF, but the mechanistic link between these processes remains unclear. Here, we identify a Kat5-STAT6 epigenetic-metabolic axis that governs fibrotic progression. Kat5 directly acetylates STAT6 at lysine 636 (K636), thereby suppressing STAT6 dimerization, phosphorylation and nuclear translocation. In fibrotic lungs, STAT6 acetylation at K636 is reduced, leading to its hyperactivation. Activated STAT6 drives transcription of pro-glycolytic enzyme hexokinase 2 (HK2), promoting metabolic reprogramming in alveolar type II (ATII) cells and extracellular matrix deposition. ATII cell-specific restoration of Kat5 rescues STAT6 acetylation, normalizes its activity and ameliorates fibrosis in vivo. Mechanistically, Kat5-mediated STAT6 acetylation functions as a biochemical brake that limits cooperation with profibrotic mediators such as tissue plasminogen activator (tPA). These findings redefine STAT6 regulation, highlight an acetylation-phosphorylation checkpoint controlling fibrogenesis, and suggest that Kat5 enhancers or STAT6 acetylation mimetics may represent potential therapeutic strategies for chronic lung disease. - Source: PubMed
Publication date: 2026/07/03
Yang YoujingLing YiLi JianzhongLi QianminFeng YanmeiXiao JunMa YuTao Shasha - Alzheimer's disease (AD) can be caused by autosomal-dominant familial Alzheimer's disease (FAD) mutations in amyloid precursor protein (APP) or presenilin-1 and 2, which form an enzyme substrate complex. KAT5 binds to the APP intracellular domain. Recent reports of decreased γ-secretase activity in FAD mutants support KAT5 membrane sequestration. - Source: PubMed
Cary Greg AYoung Jessica ERose Shannon EFrankowski HaraldWilkins HeatherAmirtha Ganesh Sai SruthiDraper JuliaDarvas MartinBothwell MarkJayadev SumanReid Aquene NGreenwood AnnaLevey Allan ILeal KarinaCarter Gregory WWiley Jesse C - Following the publication of this paper, it was drawn to the Editor's attention by a concerned reader that the GAPDH control western blots shown in Fig. 5A on p. 9 for the experiments without MG132 treatment ('‑ MMGM132') were strikingly similar to the GAPDH control western blots shown in Fig. 5D, albeit with some horizontal and vertical resizing of the bands. In addition, an independent analysis of the data in this paper revealed that the flow cytometric plots for the TIP60‑transfected cells experiment in Fig. 8B on p. 12 were also strikingly similar to the plots shown to represent the TIP60‑eGFP Positive cells experiment in Fig. 8E. The authors have been contacted by the Editorial Office to offer an explanation for the apparent re‑use of the abovementioned data in this paper, and we are awaiting their response. Owing to the fact that the Editorial Office has been made aware of potential issues surrounding the scientific integrity of this paper, we are issuing an Expression of Concern to notify readers of this potential problem while the Editorial Office continues to investigate this matter further. [International Journal of Oncology 59: 89, 2021; DOI: 10.3892/ijo.2021.5269]. - Source: PubMed
Publication date: 2026/06/26
Ahmad TanveerAshraf WaseemIbrahim AbdulkhalegZaayter LiliyanaMuller Christian DHamiche AliMély YvesBronner ChristianMousli Marc