Polyclonal DRAK2, C-Terminal
- Known as:
- Polyclonal DRAK2, C-Terminal
- Catalog number:
- pc-177
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Kamiya biomedical company
- Gene target:
- Polyclonal DRAK2 C-Terminal
Related genes to: Polyclonal DRAK2, C-Terminal
- Gene:
- STK17B NIH gene
- Name:
- serine/threonine kinase 17b
- Previous symbol:
- -
- Synonyms:
- DRAK2
- Chromosome:
- 2q32.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-21
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal DRAK2, C-Terminal
Related articles to: Polyclonal DRAK2, C-Terminal
- DRAK2 (STK17B), a serine/threonine kinase, functions as a positive regulator of apoptosis. Despite its therapeutic potential, pharmacological inhibition of DRAK2 remains underexplored. To address this gap, we leveraged the previously disclosed small-molecule DRAK2 inhibitor 22b as a chemical starting point and designed, synthesized, and evaluated a novel series of thieno[2,3-b]pyridine derivatives. Through systematic structure-activity relationship (SAR) analysis, compound I14 was identified as a lead DRAK2 inhibitor with favorable bioactivity. It exhibited improved DRAK2 inhibitory potency (IC = 198.5 nM) relative to the reference compound 22b; enhanced glucose-stimulated insulin secretion (GSIS) in mouse pancreatic islets by 1.86-fold (low dose) and 1.72-fold (high dose); elevated mitochondrial membrane potential (MMP) in INS-1E cells by 1.08-fold and 1.10-fold, respectively; and mitigated palmitic acid (PA)-induced MMP impairment and apoptosis. In vivo, I14 significantly improved glucose tolerance in an oral glucose tolerance test (OGTT). Mechanistically, I14 exerted its efficacy through modulation of the DRAK2-ULK1 signaling axis which was well established in our previous study. Molecular docking analyses further supported its target engagement, revealing stable hydrogen-bond interactions with Ala113 and Lys37 within the DRAK2 ATP-binding pocket. Collectively, these findings identify I14 as the first orally efficacious, mechanism-validated DRAK2 inhibitor with translational relevance for type 2 diabetes (T2D) therapy. - Source: PubMed
Publication date: 2026/06/03
Shu YuhangZhang BingqianZhang YuxinZhang XinwenXu HonghongLi RuihanLiu YuhongZhang YueqingXiong MaoqianTang JieLu YutingLi JingyaYang Fan - Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1 (DRAK1/STK17A) is a serine/threonine kinase of the Death Associated Protein Kinase (DAPK) family. STK17A is widely expressed and enriched in immune tissues, and is primarily localized in the nucleus, though it can translocate to the cytoplasm in response to specific stimuli. STK17A stimulates apoptosis and cytoskeletal dynamics, but its physiological roles remain incompletely defined, in part due to limited availability of potent/selective chemical probes and the absence of STK17A in commonly used rodent models. In this review, we summarize current knowledge on STK17A, including its structure, evolution, expression patterns, molecular interactions, and roles in cancer as well as in autoimmune, cardiovascular, infectious, and neurological disorders. We also compare STK17A with its closest homolog, STK17B, highlighting both shared features and functional distinctions. The review further examines recent medicinal chemistry efforts that have yielded the first small-molecule modulators of STK17A (DRAK1) and STK17B (DRAK2), including dual inhibitors and emerging selective scaffolds. These compounds can serve as valuable chemical probes and hold promising therapeutic potential. Nonetheless, challenges of selectivity and functional validation remain, emphasizing the need for continued medicinal chemistry efforts to unlock the full potential of STK17A as a therapeutic target across cancer, autoimmune, and neurodegenerative diseases. - Source: PubMed
Publication date: 2026/03/30
Gonçalves Leticia Christina PiresRastoin OliviaMorozova ViraBuzet ClémentBennetot AudreyPagès GillesRonco CyrilDufies Maeva - Natural killer (NK) cells are promising effectors for cancer immunotherapy, but their efficacy is limited by immunosuppressive tumor microenvironments. To uncover strategies for enhancing NK cell function, we establish a CRISPR loss-of-function screening platform for primary human NK cells by combining BaEVRless-pseudotyped lentiviral transduction of sgRNA libraries with Cas9 protein electroporation. This platform enables genome-scale interrogation of gene function in non-transformed NK cells. Kinome-focused and genome-wide screens identify key regulators of NK cell proliferation, cytotoxicity, and resistance to prostaglandin E (PGE)-mediated suppression. STK17B deletion enhances NK cell expansion, while loss of CCDC53 boosts degranulation and cytotoxicity. We also uncover the CRL5 complex-including RNF7, UBE2F, and CISH-as critical inhibitors of IL-2 signaling and effector function under PGE stress. These findings establish a scalable platform for CRISPR-based functional genomics in primary NK cells and reveal engineering targets to enhance NK cell persistence and efficacy in tumor microenvironments. - Source: PubMed
Publication date: 2026/04/15
Nguyen Quoc VietLan Yi-JunChang Jason Cheng-YuShih Hsin-AnFaustine JeniferChen Cheng-ChiehHo Shu-YuCheng Ching-WenChao Tsu-LanLin Steven - [This corrects the article DOI: 10.21037/atm-21-601.]. - Source: PubMed
Publication date: 2025/01/15
- - Source: PubMed
Liu Bei