KAT5 pSer90 antibody Ab host: Rabbit
- Known as:
- KAT5 pSer90 (anti-) Antibody production species: Rabbit
- Catalog number:
- 'A8434-1
- Product Quantity:
- 50 Вµg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- KAT5 pSer90 antibody host: Rabbit
Related genes to: KAT5 pSer90 antibody Ab host: Rabbit
- 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
- Gene:
- PPP1R18 NIH gene
- Name:
- protein phosphatase 1 regulatory subunit 18
- Previous symbol:
- KIAA1949
- Synonyms:
- phostensin
- Chromosome:
- 6p21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-02
- Date modifiied:
- 2016-10-05
Related products to: KAT5 pSer90 antibody Ab host: Rabbit
Related articles to: KAT5 pSer90 antibody Ab host: Rabbit
- 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 - Prostate adenocarcinomas (PRAD) can acquire resistance to androgen receptor signaling inhibitors through lineage transition to a cell state known as neuroendocrine prostate cancer (NEPC). Using a panel of isogenic PRAD and NEPC mouse tumoroids, we show that NEPC cells acquire new transcription factor (TF) dependencies that function in a previously undefined network. Through selective perturbation of each TF, we identify ASCL1 as a key regulator of NE lineage fate whereas MYCL functions downstream to drive NEPC growth/survival by recruitment of the TIP60/KAT5 acetyltransferase. Interestingly, while dependencies on specific TF family paralogs can vary across NEPC models, all show markedly enhanced dependency on TIP60. Moreover, the H2A.Z-acetyltransferase activity of the TIP60 complex (TIP60-C) is required for NEPC as well as the acetyl-reader BRD8, which is newly incorporated as a TIP60-C subunit with the NEPC transition. Targeted degradation studies in isogenic tumoroids reveal increased dependence on MYCL in NEPC relative to its paralog MYC in PRAD. In addition to a paralog switch (MYC to MYCL), the MYC pathway-addicted NE state is accompanied by a chaperone switch (from TIP60-C to SRCAP) for H2A.Z histone exchange and a coactivator switch (to TIP60) for MYC target gene expression. The NE-specific coupling of MYCL with TIP60 reveals a previously unappreciated opportunity to target MYC-driven NE diseases through pharmacological inhibition of TIP60. - Source: PubMed
Publication date: 2026/05/08
Sun ZhenZhao Jimmy LKhan Zahra FIsmail Wazim MHan TengNandakumar SubhikshaYoung SerinaLange MatthewCheng PanKoche RichardSchultz NikolausGaspar-Maia AlexandreSawyers Charles L - Aortic aneurysm (AA) is a life-threatening vascular disorder characterized by smooth muscle cell (SMC) phenotypic switching. However, SMC heterogeneity and the regulatory mechanisms underlying this transition remain incompletely understood. - Source: PubMed
Publication date: 2026/05/14
Zhang JianlinZhao Wenbo - MYST lysine acetyltransferases (KATs) are a class of epigenetic enzymes critical for cellular function that constitute an emerging therapeutic target in cancer. Recently, several drug-like MYST inhibitors have been reported that show promise in preclinical models as well as in clinical trials of breast cancer. Understanding the specificity of these molecules is critical for their effective use as chemical probes. Here we apply an integrated profiling strategy to systematically define the potency and selectivity of drug-like MYST KAT inhibitors. First, we use optimized chemoproteomic profiling and histone acetylation biormarkers to study the industry-developed KAT inhibitor PF-9363. This reveals dose-dependent engagement of native KAT complexes, with hierarchical inhibition following the order KAT6A/B > KAT7 » KAT8 > KAT5. This pattern of target engagement is shared by the clinical candidate PF-8144. Next, we demonstrate how PF-9363's ability to disrupt capture of MYST complex members in chemoproteomic experiments can be leveraged to identify uncharacterized candidate members of these complexes, including the transcription factor FOXK2. Applying insights from these studies to WM-8014, WM-1119 and WM-3835, which have been extensively applied in the literature as MYST probes, highlights unexpected cross-inhibition and suggests a framework for how these small molecules and biomarkers may be applied to differentiate KAT6A/B and KAT7-dependent phenotypes. Finally, we benchmark the activity of PF-9363 in the NCI-60 cell line screen, providing evidence that its ability to engage KAT8 at elevated concentrations can drive acute growth inhibition. Collectively, our studies indicate the potential for MYST KAT inhibitors, including clinical candidates, to exhibit dose-dependent target engagement reminiscent of kinase inhibitors. The assays and biomarkers described here should find broad utility in assessing selective target engagement by this inhibitor class. - Source: PubMed
Publication date: 2026/05/13
Chen XueminCastroverde AlexandraPerez MinervoHolewinski RonaldSuazo Kiall FKarki RashmiAndresson ThorkellGarcia Benjamin AMeier Jordan L