Recombinant Human Cell Division Cycle 25A CDC25A
- Known as:
- Recombinant Human Cell Division Cycle 25A CDC25A
- Catalog number:
- enz-091
- Product Quantity:
- 1
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- Recombinant Human Cell Division Cycle 25A CDC25A
Related genes to: Recombinant Human Cell Division Cycle 25A CDC25A
- Gene:
- CDC25A NIH gene
- Name:
- cell division cycle 25A
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1992-07-31
- Date modifiied:
- 2017-12-06
Related products to: Recombinant Human Cell Division Cycle 25A CDC25A
Related articles to: Recombinant Human Cell Division Cycle 25A CDC25A
- Premature ovarian failure (POF) is closely linked to ovarian granulosa cell (OGC) senescence and cell cycle arrest. This study explored the role of the miR-322/Klotho axis in OGC aging. Using a cyclophosphamide-induced mouse model and cultured OGCs, we found Klotho significantly downregulated in POF, inversely correlating with elevated miR-322 and senescence markers p16, p21, and p53. Luciferase assays confirmed Klotho as a direct miR-322 target. miR-322 overexpression induced G0/G1 and G2/M phase arrest and OGC senescence by silencing Klotho, while miR-322 inhibition partially rescued the POF phenotype. miR-322 knock-in mice exhibited reduced ovarian weight, increased follicular atresia, and altered E2/FSH levels, mimicking clinical POF. Mechanistically, the miR-322/Klotho axis modulated cell cycle regulators, upregulating CHK1 and downregulating CDC25A, CDK2, and Cyclin A/E. Thus, miR-322 promotes OGC senescence and POF by targeting Klotho to activate cell cycle inhibition pathways, identifying this axis as a critical epigenetic regulator of ovarian aging and a potential therapeutic target. - Source: PubMed
Publication date: 2026/09/09
Cui ZeyuLai YanchenChen XiangfengWang ChunxiaZhang BimengLiu Te - Oral squamous cell carcinoma (OSCC) is characterized by aggressive growth and frequent recurrence, highlighting the need for novel targeted therapies. Magnolol, a bioactive compound derived from , exhibits anti-tumor activity. In this study, we synthesized a methoxylated derivative, 2-O-methylmagnolol (MM1), and evaluated the anti-OSCC efficacy and underlying mechanisms of magnolol and MM1. - Source: PubMed
Publication date: 2026/07/01
Chen Chi-YuanShieh Tzong-MingChen Chin-ChuanLeu Yann-LiiChu Yu-DeLiou Miaw-JeneLiu Yi-TsenLin Hsin-WeiChen Kai-YinYu Cheng-ChiaWang Tong-Hong - Glioblastoma (GBM) is among the most aggressive primary brain tumors, marked by rapid proliferation, therapeutic resistance, and profound intratumoral heterogeneity. Epigenetic regulators such as lysine-specific demethylase 1A (KDM1A) and histone deacetylase 2 (HDAC2) are aberrantly expressed in resistant GBM subpopulations and strongly correlate with poor clinical outcomes. Here, we assessed the therapeutic potential of MPT0G521, a dual KDM1A/class I HDAC inhibitor, in disrupting epigenetic regulation and cell cycle progression. Bioinformatic analyses of resistance-associated gene profiles (temozolomide and 2 Gy radiation) and single-cell transcriptomic datasets from distinct tumor regions revealed enrichment of KDM1A and HDAC2 in high-cycling GBM clusters, particularly at invasive margins prone to recurrence. Functional assays demonstrated that MPT0G521 potently inhibited proliferation of both parental and temozolomide-resistant GBM cells, inducing G2/M arrest and apoptosis. Transcriptomic profiling further identified significant downregulation of centrosome integrity genes (FSD1, KIFC1), spindle regulators (TUBB, STMN1, KIF2C, KIF15), kinetochore components (AURKB, CDCA8, SPAG5), and G2/M checkpoint mediators (CENPF, MYBL2, CCNF, MYT1, CDC25A), resulting in disrupted mitotic progression. Mechanistically, MPT0G521 increased histone H3 methylation and acetylation, validating its dual inhibitory activity against KDM1A and class I HDACs. Collectively, these findings indicate that MPT0G521 disrupts the G2/M activation and mitotic machinery, thereby suppressing proliferative and resistant GBM subpopulations. This dual epigenetic strategy holds strong promise for overcoming GBM heterogeneity and reducing recurrence. - Source: PubMed
Publication date: 2026/09/02
Wu An-ChihChuang Jian-YingLiu Jr-JiunSalim Enrica AngelinaWu Ming-HsiaoJing Shih-WeiHsu Tsung-IChang Kwang-YuChang Wen-ChangThakur AmandeepLiou Jing-PingLo Wei-Lun - The review covers research on dual-target antitumor agents over the past five years. One of the targets is histone deacetylases (HDACs), while the second potential target is a protein group located both on the membrane surface (phosphatidylinositol 3-kinase (PI3K), anaplastic lymphoma kinase (ALK), receptor tyrosine kinase (AXL), tyrosine protein kinase (HER2), FMS-like tyrosine kinase (FLT3), and vascular endothelial growth factor receptor (VEGFR2)) and in the nucleus (serine/threonine protein kinase Wee1, DNA methyltransferase (DNMT), dual-specificity phosphatase (CDC25A), an enzyme from the cyclin-dependent kinase family (CDK9), dual-specificity tyrosine-serine/threonine kinase (DYRK2), and BET family proteins (BRD4, BD1, and BD2)). This review presents the results of studies on the inhibitory activity of various HDAC isoforms and other enzymes, as well as in vitro cytotoxicity studies on both neoplastic and healthy cells. It also includes selectivity studies, in vivo experiments (changes in tumor volume in mice) and oral bioavailability assessments. The review also describes the chemical structures of several dual-target agents and identifies the molecular fragments responsible for inhibiting different targets. Based on the studies reviewed in this paper, it can be concluded that some dual inhibitors have superior in vitro cytotoxicity and exhibit selectivity towards some tumor cells compared to monofunctional reference compounds. These findings may be useful for molecular design in the field of polypharmacology, with the aim of developing new dual-target molecules that exhibit improved antitumor activity and selectivity towards neoplastic cells. - Source: PubMed
Publication date: 2026/07/24
Yudaev PavelAleksandrova YuliaNeganova Margarita - Hepatocellular carcinoma (HCC) is a leading cause of cancer death, yet immune checkpoint inhibitors (ICIs) benefit only a minority of patients-a limitation attributed to low tumor mutational burden (TMB) and an immunologically cold microenvironment. SMG1, a serine/threonine kinase of the phosphatidylinositol 3-kinase-related kinase (PIKK) superfamily, sits at the intersection of RNA surveillance, the DNA damage response, and oncogenic signaling. As the master kinase of nonsense-mediated mRNA decay (NMD), SMG1 phosphorylates UPF1 to degrade transcripts bearing premature termination codons; independently, it restrains tumor growth by phosphorylating p53 (Ser15) and promoting Cdc25A turnover. SMG1 was originally identified as a tumor-suppressive modulator of sorafenib resistance in HCC (Nam, S.W. et al., 2014), and subsequent work shows SMG1 is reduced in HCC, predicts adverse outcome, and is recurrently silenced by reversible promoter hypermethylation. Paradoxically, the same kinase conceals mutation-derived neoantigens, and its selective inhibition (e.g., KVS0001) raises HLA class I neoantigen presentation toward high-TMB levels and improves checkpoint-inhibitor efficacy in preclinical and liver-specific models. This critical review integrates SMG1 structural biology, clinicopathology, signaling, sorafenib resistance, and NMD-directed immunotherapy, grading established versus inferential mechanisms, and nominates SMG1 and NMD as dual, context-dependent targets for HCC precision oncology. - Source: PubMed
Publication date: 2026/07/31
Nam Soon Woo