Polyclonal Rabbit Histone acetyltransferase KAT5 Antibody (Biotin)
- Known as:
- Polyclonal Rabbit Histone acetyltransferase KAT5 Antibody (Biotin)
- Catalog number:
- abx105518
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- Polyclonal Rabbit Histone acetyltransferase KAT5 Antibody (Biotin)
Related genes to: Polyclonal Rabbit Histone acetyltransferase KAT5 Antibody (Biotin)
- 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: Polyclonal Rabbit Histone acetyltransferase KAT5 Antibody (Biotin)
Related articles to: Polyclonal Rabbit Histone acetyltransferase KAT5 Antibody (Biotin)
- Immunotherapy has shown promising efficacy in esophageal squamous cell carcinoma (ESCC), yet its clinical benefits remain limited due to immune evasion. Lactate accumulation in the tumor microenvironment has been found to facilitate immune evasion through protein lactylation. However, the key lactylated substrates and mechanisms driving immune evasion remain undefined. Here, we show that HSPA1A lactylation at lysine 108 (K108) by KAT5 drives CD8⁺ T cell dysfunction and immunotherapy resistance via the STAT1/PD-L1 axis in ESCC. Mechanistically, K108 lactylation enhances HSPA1A binding to STAT1, protecting STAT1 from TRIM25-mediated ubiquitination and proteasomal degradation. This stabilization promotes STAT1 phosphorylation and nuclear translocation, leading to transcriptional upregulation of PD-L1 and subsequent immune evasion. Collectively, these findings highlight the pivotal role of HSPA1A lactylation in facilitating immune evasion via the STAT1/PD-L1 axis, suggesting a potential target for improving immunotherapy efficacy in ESCC. - Source: PubMed
Publication date: 2026/09/24
Wang ZiyiLi XinyanLuo PengLi SuXu YanLi WenyaLiu QuanxingChen YuqiongSun Xiangyu - Rapid repair of genotoxic therapy induced DNA damage mediates treatment resistance in glioblastoma (GBM). The role of non-malignant cell types in the tumor microenvironment in accelerating DNA repair in neoplastic cells is poorly understood. Using spatial transcriptomics, immunofluorescence, metabolomics, patient tissues and preclinical models, we show that tumor associated macrophages (TAMs) in GBM promote DNA repair and treatment resistance in neoplastic cells through the secretion of acetylated amino acids. These acetylated amino acids are consumed by GBM cells, leading to enhanced acetyl Co-A levels, histone acetylation and nucleotide synthesis. Interrupting histone acetylation via inhibition of the acetyltransferase KAT5 breaks these metabolic links and reverses the protective capacity of microenvironment-derived acetylated amino acids and TAMs. Blocking the exchange of acetylated amino acids and their downstream effects is a potential strategy for the treatment of GBM. - Source: PubMed
Publication date: 2026/09/18
Wahl DanielSravya PalavalasaAltay LeylaDo KathyFreeman JackGokul AditriLiang NingningScott AndrewXu JieKorimerla NavyatejaLin AngelicaWang HengWilder-Romans KariSinger AvaO'Brien AlexandraAnimasahun OlamideMeghdadi BaharanBaker EmilyPeterson ErikMcCulla ElizabethZhu ZiqingThomas DafyddAndren AnthonyWong HarrisonSajjakulnukit PeterZhang LiShankar SunitaRavikumar VisweswaranLee Zheng HongCarrion Joseph NietoBhadury SagnikMiller CJann SarkariaHeth JasonHuse JasonCamelo-Piragua SandraMorgan MeredithLawrence TheodoreRao ArvindLyssiotis CostasAl-Holou WajdNagrath DeepakZhou Weihua - Abnormal epigenetic modifications are involved in central nervous system (CNS) diseases. Histones play a crucial role in chromatin structure and function, whose post-translational modifications significantly impact gene expression and chromatin dynamics. Histone acetylation, governed by the balance between histone acetyltransferases (HATs) and histone deacetylases (HDACs), is one of the key modulators of chromatin accessibility and transcriptional activity. Lysine acetyltransferase 5 (KAT5, aka TIP60), a member of the MYST subfamily of HATs, is involved in many cellular processes, including DNA repair, apoptosis, and cell cycle control. Notably, the dysfunction of KAT5 has been implicated in several CNS diseases. In this review, we explored the roles of KAT5 in CNS pathophysiology, emphasizing its involvement in neurological disorders and its potential as a therapeutic target. This review sheds light on the epigenetic mechanisms in CNS diseases mediated by KAT5 and provides valuable information for potential treatment strategies. - Source: PubMed
Publication date: 2026/09/03
Xin XiaomingWu LingjuanLiu MeichenLiu TianYuan ZihanZhang LiangDuan TongqingZhang LeiZhu Xianmin - Inflammation is a pivotal driver of the progression from metabolic dysfunction-associated steatotic liver disease (MASLD) to metabolic dysfunction-associated steatohepatitis (MASH), an aggressive form associated with substantial liver-related mortality. However, the molecular mechanisms underlying the initiation and persistence of liver inflammation remain poorly defined. Here, we demonstrated a previously unrecognized role for hepatic acetyl-CoA synthetase short-chain family member 2 (ACSS2) in MASH, showing that ACSS2 upregulation in patients exacerbates MASH progression by functioning as an epigenetic regulator, independent of its canonical lipogenic role. Mechanistically, ACSS2, in complex with lysine acetyltransferase 5 (KAT5), upregulates allograft inflammatory factor-1 (AIF1) transcription via histone crotonylation, thereby inducing liver inflammation and subsequently resulting in the aberrant accumulation of senescent hepatocytes, which further enhances proinflammatory cytokine production. This ultimately initiates a vicious cycle of chronic inflammation, which directly promotes the progression from simple steatosis to MASH. Thus, our work reveals a mechanistically defined and pivotal role for ACSS2 in promoting the MASLD-to-MASH transition, highlighting its potential as a compelling therapeutic target. - Source: PubMed
Publication date: 2026/07/25
Wen XiaoWu KeyanWang MengyaoMa ZihanWang TaoZhang JingWang BeiChen SiyuanWang JingyiChen SiyueYang FanLiu ChuweiChen XianyangDeng LuCheng YafanMiao Qing RobertSun BaofaRuan XiongzhongLi KaiDuan YajunHu Wenquan - Thyroid cancer (THCA) is the most common endocrine malignancy worldwide, understanding the pathophysiological mechanism is vital for developing effective strategies for prevention, diagnosis, and treatment. In this study, paired tumor and adjacent noncancerous tissues were collected from THCA patients. Cell viability and proliferation were assessed using CCK-8 and EdU assays. Cell migration and invasion were evaluated by wound healing and Transwell assays. Co-immunoprecipitation was performed to examine RNF123-mediated KAT5 ubiquitination, and chromatin immunoprecipitation was used to assess KAT5 enrichment at the PSPC1 promoter. An experimental lung metastasis model was established to evaluate the effects of RNF123 overexpression on tumor growth and pulmonary metastasis. RNF123 was down-regulated in THCA tissues and cell lines, and its overexpression suppressed cell viability, proliferation, migration, and invasion. KAT5 and PSPC1 were up-regulated in THCA cells. KAT5 knockdown inhibited THCA malignant behaviors. Mechanistically, RNF123 promoted the ubiquitination and degradation of KAT5, thereby reducing KAT5-mediated histone acetylation at the PSPC1 promoter and subsequent IGF1R up-regulation. In conclusion, RNF123 inhibited THCA malignant phenotype by promoting KAT5 ubiquitination and degradation, which reduced KAT5-mediated histone acetylation at the PSPC1 promoter, thereby down-regulating PSPC1 and IGF1R expressions. - Source: PubMed
Publication date: 2026/08/23
Guo LinJiang SenheWang XuehanFeng YirenJin Gang