CDC2L5 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- CDC2L5 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb101416
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- CDC2L5 antibody Polyclonal Antibodies Primary antibodies
Related genes to: CDC2L5 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- CDK13 NIH gene
- Name:
- cyclin dependent kinase 13
- Previous symbol:
- CDC2L5
- Synonyms:
- CHED, CDC2L, KIAA1791
- Chromosome:
- 7p14.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-18
- Date modifiied:
- 2016-06-08
Related products to: CDC2L5 antibody Polyclonal Antibodies Primary antibodies
Related articles to: CDC2L5 antibody Polyclonal Antibodies Primary antibodies
- Nucleoside analogues are traditionally developed as antimetabolites that interfere with nucleic acid synthesis after intracellular phosphorylation. In this study, inspired by the 3',4'-unsaturated sugar scaffold of ddhCTP, we designed and synthesized a series of 3',4'-unsaturated nucleoside analogues to explore their antiproliferative potential and possible non-classical cellular effects. Among the synthesized compounds, 17k, a C-nucleoside bearing both a 3',4'-unsaturated sugar moiety and a chlorinated remdesivir-like base, exhibited potent antiproliferative activity against HepG2 cells, with an IC₅₀ value of 2.27 ± 0.36 μM, lower than that of gemcitabine under the same assay conditions. In the nonmalignant GES-1 epithelial cell line, 17k showed an IC₅₀ value of 34.26 ± 3.45 μM, corresponding to a selectivity index of 15.1 relative to HepG2 cells. Closely related compounds 12 and 17j showed no detectable activity, indicating a narrow structure-activity relationship. Exploratory single-concentration kinase profiling at 20 μM showed strong inhibition of several transcription-associated CDK/cyclin complexes (CDK13/CycK, CDK12/CycK, CDK9/CycT1, CDK19/CycC, and CDK8/CycC) and selected receptor tyrosine kinases (KDR/VEGFR2, RET, EPHA1, and FLT3). Compound 17k also suppressed colony formation and wound closure, induced apoptosis, and caused S-phase accumulation in HepG2 cells. These findings identify 17k as a nucleoside analogue with unanticipated antiproliferative activity and suggest that kinase modulation may contribute to its cellular effects. - Source: PubMed
Publication date: 2026/08/14
Wang SongYang JingYang XinyueHuang HaoZou HaiyangZhang YuZhang XushanLuo CongcongZhao BingLiu Feng-WuHerdewijn Piet - The ovarian cancer immunoreactive antigen domain-containing protein 1 (OCIAD1) is a mitochondrial protein implicated in mitochondrial morphology, energy metabolism, and differentiation. Although understudied, recent studies position it as a critical player in carcinogenesis and neurodegenerative disorders, making it a potentially druggable node in cellular signaling networks. However, the phosphoregulatory networks and the upstream kinases governing OCIAD1 remain unknown. - Source: PubMed
Publication date: 2026/07/23
Fahma AmalSubair SuhailLubaba FathimathulGopalakrishnan Athira PerunellyShivamurthy Prathik BasthikoppaRaju Rajesh - Cyclin-dependent kinase 12 (CDK12) is a transcription-associated kinase critical in regulating transcription, mRNA splicing, translation, cell cycle progression, and DNA damage repair (DDR) pathways. CDK12 is a notable therapeutic target in cancer owing to its regulation of key DDR genes, including BRCA1 and BRCA2, which are essential in maintaining genomic stability. In this study, we describe the lead optimization of a 1,4--cyclohexane-based series, resulting in the discovery of a novel and highly selective CDK12 inhibitor, CTX-439. CTX-439 demonstrated robust CDK12 inhibition, sustained potency against its homologous protein CDK13, and outstanding selectivity over other CDKs and the broader kinome. A comprehensive evaluation, including ADME-Tox profiling, identified CTX-439 as a promising drug candidate for targeted cancer therapy. - Source: PubMed
Publication date: 2026/06/23
Shimokawa KenichiroOno KojiAsano MoriteruHirayama TakaharuTokuhara HidekazuTanaka ToshioBanno HiroshiSakauchi NobukiHirata YasuhiroFujimoto JunKokubo HironoriMizojiri RyoCary Douglas RIto MasahiroMaezaki HironobuImaeda YasuhiroTanaka HiroshiUchiyama NorikoSameshima TomoyaKondo MitsuyoKawamoto TomohiroSugiyama MidoriYamakawa HirokoMorishita DaisukeArikawa Yasuyoshi - Targeting transcriptional condensates is an emerging paradigm for cancer therapy. A key player is the transcriptional coactivator YAP (Yes-associated protein), which drives tumor-specific programs that fuel tumor progression and therapeutic resistance. Cyclin K, partnered with cyclin-dependent kinases (CDKs) CDK12/CDK13, is essential for transcription elongation, but its role in specific oncogenic programs was unclear. Here, we identify Cyclin K as an essential vulnerability across multiple cancer types. The CDK12/Cyclin K complex binds YAP via Cyclin K and forms a regulatory condensate to bridge YAP phosphorylation by CDK12. Such a phosphorylation at threonine-398 impedes YAP inhibition by its canonical LATS kinases, stabilizes YAP, and enables its further condensation with TEAD4 to stimulate YAP oncogenic activity. Coexpression of CDK12/Cyclin K and YAP predicts sensitivity to Cyclin K inhibitors in hepatocellular carcinoma cells and patient-derived xenografts. Thus, we define CDK12/Cyclin K as a critical regulator of YAP-driven transcriptional addiction and a biomarker for patient stratification who mostly benefit from therapies targeting the CDK12/Cyclin K-YAP axis. - Source: PubMed
Publication date: 2026/07/03
Sun YangZhang YuYan WeikangDuan JinlinQiao KeYan GuoquanXue JunyanWang JieZhan MingLi QiweiWang HongchengZhang Yonglong - Cyclin-dependent kinase (CDK) 12 and its paralog, CDK13, phosphorylate RNA polymerase II, enabling transcriptional elongation. In solid tumors, CDK12 loss promotes progression by inducing replication-transcription conflict and fueling genomic instability. However, we have uncovered upregulation of CDK12 and CDK13 in ~5% of colorectal cancer (CRC) specimens, suggesting a role in cancer cell survival. Based on this, we postulated that CDK12/13 inhibition in CRC may represent a useful therapeutic strategy. To test this, we screened CDK12 and CDK12/13 inhibitors across multiple cancer cell lines and patient-derived organoids (PDO) from a range of solid tumors, demonstrating potent activity in CRC PDO. Using siRNA-mediated knockdown, we identified CDK13 as a potential mechanism of resistance to CDK12-specific inhibition. Mechanistically, CDK12/13 inhibition led to a decreased abundance of BRCA1 long transcripts, rendering cells susceptible to combination therapy with PARP inhibitors. To further assess the clinical utility of CDK12/13 inhibition, we focused on CRC, for which there is an urgent need for additional therapies. We tested the efficacy of CT7439, a novel CDK12/13 inhibitor and cyclin K degrader, which showed cytotoxicity in the low nanomolar range, reduced BRCA1 expression, and concomitant DNA damage. Together, our data support further clinical development of CDK12/13 inhibition in CRC. - Source: PubMed
Publication date: 2026/06/30
Watlington Wylie KDayanidhi Divya LZokaasadi MohammadMantyh John BOlawuni Pelumi DRupprecht GabrielleForce Jeremy MMcCall ShannonBahl Ashwani KHsu David SSomarelli Jason A