Goat Anti-Human DRAK 1
- Known as:
- Goat Antibody toHuman DRAK 1
- Catalog number:
- 129-10265
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Ray Biotech
- Gene target:
- Goat Anti-Human DRAK 1
Related genes to: Goat Anti-Human DRAK 1
- Gene:
- STK17A NIH gene
- Name:
- serine/threonine kinase 17a
- Previous symbol:
- -
- Synonyms:
- DRAK1
- Chromosome:
- 7p13
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-21
- Date modifiied:
- 2014-11-19
- 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: Goat Anti-Human DRAK 1
Related articles to: Goat Anti-Human DRAK 1
- 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 - The serine/threonine kinase 17B (STK17B) is involved in setting the threshold for T cell activation and its absence sensitizes T cells to suboptimal stimuli. Consequently, STK17B represents an attractive potential target for cancer immunotherapy. - Source: PubMed
Publication date: 2024/10/21
Scheuplein FelixRenner FlorianCampbell John ECampbell RobertDe Savi ChrisEckmann JanFischer HolgerGe JieGreen LukeJakob PeterKim Joseph LKinkema CaitlinMcGinn KatieMedina RicardoMüller AnnemariePerez NishaPerola EmanueleTimsit YoavTraore TaryHopfer UlrikeTyanova StefkaTzouros ManuelWang RuduanWoessner RichardDorsch MarionBischoff James R - STK17A is a novel uncharacterized member of the death-associated protein family of serine and threonine kinases. Overexpression of STK17A is observed in many cancers. We identified a lead compound that is based on a quinazoline core. Optimizations of the lead compound led to the discovery of potent and selective STK17A/B inhibitors with drug-like properties and oral bioavailability. Compound had an STK17A inhibitory IC of 23 nM. Based on profiling studies against two wild-type kinase panels (375 and 398 kinases, respectively), compound had strong inhibition of both STK17A and STK17B but moderate off-target inhibition only for AAK1, MYLK4, and NEK3/5. In addition, compound had good oral bioavailability, paving the way for in vivo studies against various cancers. - Source: PubMed
Publication date: 2024/05/20
Chaudhry SanaCastro Jesus RTotiger Tulasigeri MAfaghani JumanaKhurshid RabiaNicholls MiahZhang ZimingSchürer Stephan CShah AshishTaylor JustinFeng Yangbo - As a member of the death-associated protein kinase (DAPK) family, STK17B plays an important role in the regulation of cellular apoptosis and has been considered as a promising drug target for hepatocellular carcinoma. However, the highly conserved ATP-binding site of protein kinases represents a challenge to design selective inhibitors for a specific DAPK isoform. In this study, molecular docking, multiple large-scale molecular dynamics (MD) simulations, and binding free energy calculations were performed to decipher the molecular mechanism of the binding selectivity of PKIS43 toward STK17B against its high homology STK17A. MD simulations revealed that STK17A underwent a significant conformational arrangement of the activation loop compared to STK17B. The binding free energy predictions suggested that the driving force to control the binding selectivity of PKIS43 was derived from the difference in the protein-ligand electrostatic interactions. Furthermore, the per-residue free energy decomposition unveiled that the energy contribution from Arg41 at the phosphate-binding loop of STK17B was the determinant factor responsible for the binding specificity of PKIS43. This study may provide useful information for the rational design of novel and potent selective inhibitors toward STK17B. - Source: PubMed
Publication date: 2022/07/21
Liu ChangZhang YichiZhang YuqingLiu ZonghanMao FeifeiChai Zongtao - STK17B is a member of the death-associated protein kinase family and has been genetically linked to the development of diverse diseases. However, the role of STK17B in normal and disease pathology is poorly defined. Here, we present the discovery of thieno[3,2-d] pyrimidine (), a high-quality chemical probe for this understudied "dark" kinase. is an ATP-competitive inhibitor that showed remarkable selectivity over other kinases including the closely related STK17A. X-ray crystallography of and related thieno[3,2-d]pyrimidines bound to STK17B revealed a unique P-loop conformation characterized by a salt bridge between R41 and the carboxylic acid of the inhibitor. Molecular dynamic simulations of STK17B revealed the flexibility of the P-loop and a wide range of R41 conformations available to the apo-protein. The isomeric thieno[2,3-d]pyrimidine () was identified as a negative control compound. The >100-fold lower activity of on STK17B was attributed to the reduced basicity of its pyrimidine N1. - Source: PubMed
Publication date: 2020/11/20
Picado AlfredoChaikuad ApiratWells Carrow IShrestha SafalZuercher William JPickett Julie EKwarcinski Frank ESinha Parvathide Silva Chandi SZutshi ReenaLiu ShubinKannan NatarajanKnapp StefanDrewry David HWillson Timothy M