DAPK2 polyclonal antibody
- Known as:
- DAPK2 pab (anti-)
- Catalog number:
- PAB14566
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- DAPK2 polyclonal antibody
Related genes to: DAPK2 polyclonal antibody
- Gene:
- DAPK2 NIH gene
- Name:
- death associated protein kinase 2
- Previous symbol:
- -
- Synonyms:
- DRP-1, MGC119312
- Chromosome:
- 15q22.31
- Locus Type:
- gene with protein product
- Date approved:
- 1999-10-19
- Date modifiied:
- 2016-10-05
Related products to: DAPK2 polyclonal antibody
Related articles to: DAPK2 polyclonal antibody
- Alzheimer's disease (AD) is a chronic progressive neurocognitive disorder manifested by increased production and deposition of amyloid beta (Aβ), abnormal tau phosphorylation, and formation of neurofibrillary tangles (NFTs). In addition, the disease progression is found to be associated with neuronal cell death, elevated levels of reactive oxygen species, mitochondrial dysfunction, and loss of synaptic plasticity in specific regions of the brain. AD is seventh leading cause of death and over more than 70%-80% of 57 million people having dementia develop AD worldwide. The disease population is also severely increasing at an alarming rate globally. The currently available treatment strategies remain insufficient to cure the disease because AD involves very complex pathways during its progression. Death-associated protein kinase 1 (DAPK1) is identified as a promising next-generation therapeutic drug target for the management of AD. It belongs to a family of serine/threonine kinases that influences different hypotheses involved in AD pathogenesis, such as tauopathies, Aβ hypothesis, redox, and autophagy pathways. In this review, we highlight the involvement of DAPK1 in various molecular pathways associated with AD pathogenesis and the crosstalk between DAPK1 and synaptic dysfunction and neuronal cell death implicated in AD. Moreover, the various small molecules, microRNAs, and phytoconstituents have been discussed, which have the potential to be developed as a treatment strategy targeting DAPK1-related pathological pathways in AD. - Source: PubMed
Publication date: 2026/05/22
Shukla ShashikeshSingh Rakesh Kumar - Alzheimer's disease (AD) is a neurodegenerative disorder that is caused by multiple factors, characterized by a progressive decline in cognitive ability, extracellular amyloid-β (Aβ) plaques, and intracellular neurofibrillary tangles composed of hyperphosphorylated tau. Current treatment strategies can provide only symptomatic treatment or limited efficacy, highlighting the need to intervene in the upstream regulatory factors that drive both amyloid and tau pathologies. Death-associated protein kinase 1 (DAPK1) is a key driver upstream of both amyloid precursor protein processing and tau phosphorylation, simultaneously promoting amyloidogenesis and tau-mediated pathology in AD. In this study, we developed CP1, a bifunctional proteolysis-targeting chimera (PROTAC), to recruit E3 ubiquitin ligase to DAPK1, thereby inducing the ubiquitination and proteasomal degradation of DAPK1. CP1 efficiently eliminated the DAPK1 protein in primary cortical neurons without affecting its mRNA level, resulting in reduced Aβ generation and tau hyperphosphorylation. , upon systemic administration, CP1 effectively crossed the blood-brain barrier, degraded DAPK1, and consequently reduced the Aβ plaque burden and mitigated neuroinflammation in female 5xFAD mice. In a AAV-hTau-P301L tauopathy model, CP1 treatment suppressed tau hyperphosphorylation, preserved NeuN- and MAP2-positive neurons, attenuated astrocytic and microglial activation, and ultimately restored learning and memory abilities in both male and female mice. In summary, these findings demonstrate that degrading DAPK1 via a PROTAC strategy simultaneously mitigates both amyloid and tau pathology, indicating that CP1 is an effective candidate for disease-modifying therapy. - Source: PubMed
Publication date: 2026/04/23
Li RuomengYao JingPeng WenZheng LizhenWu XueyinShui XindongZheng XiaoqingTian WujinWang LongZhou YingRuan XinglinPan XiaodongZhang TaoLiu YangLee Tae HoChen Dongmei - Disuse osteoporosis, a consequence of prolonged mechanical unloading, is characterized by bone loss and elevated fracture susceptibility. Although melatonin exhibits bone‑anabolic properties, its mechanistic role in the context of mechanical unloading remains elusive. Our findings demonstrate that melatonin promotes osteogenic differentiation and suppresses osteoblast apoptosis, collectively mitigating unloading‑induced osteoporotic bone loss in hindlimb unloading (HLU) mice. Moreover, unloading suppressed YTHDF3 expression in osteoblasts and bone tissue, which was effectively rescued by melatonin administration. Functionally, YTHDF3 potentiated osteoblast differentiation and matrix mineralization while inhibiting apoptotic cell death. At the molecular level, YTHDF3 directly recognized mA‑modified Dapk2 transcripts and promoted their decay. DAPK2 was characterized as a negative regulator that impedes osteoblast differentiation and survival. Genetic analyses established that melatonin‑driven suppression of DAPK2 and functional recovery of osteoblasts are contingent upon YTHDF3. In summary, we delineate a melatonin/YTHDF3/DAPK2 protective axis that safeguards against unloading‑induced bone deterioration via post‑transcriptional regulation of Dapk2, thereby unveiling new mechanistic perspectives and therapeutic opportunities for disuse osteoporosis. - Source: PubMed
Sun QuanXu LiqunLi ZhikuiZhang JunfeiZhao XiranZhang LijunZhang XiaoyanZhao JiangdongTan YingjunWang LuyaoZhang GeHu ZebingZhang ShuShi Fei - 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 - Vestigial-like family member 3 (VGLL3), a transcriptional cofactor of the TEA domain family, has been previously identified as a regulator of osteoblast differentiation. Building upon our previous findings, we investigated VGLL3 function in MC3T3-E1 osteoblasts using an integrated approach combining transcriptomic analysis and functional assays to identify its downstream effectors and explore associated autophagy mechanisms. RNA-seq analysis of Vgll3-knockdown (shVgll3) cells identified death-associated protein kinase 2 (DAPK2), a regulator of autophagy, as a downstream effector. Autophagic activity was examined using transmission electron microscopy and western blot analysis of LC3-II and p62 proteins. The effects of Dapk2 knockdown (shDapk2) on osteoblast differentiation were evaluated using qPCR, western blotting, alkaline phosphatase staining, and Alizarin Red staining. Rapamycin treatment was used to determine whether pharmacologic activation of autophagy could restore osteoblast function. Vgll3 knockdown significantly suppressed autophagic flux, as evidenced by fewer autophagic vacuoles, decreased LC3-II accumulation, and increased p62 expression. A comparable reduction in autophagic activity was observed in shDapk2 cells and was accompanied by impaired osteoblast differentiation. Rapamycin treatment partially restored autophagy and osteogenic differentiation in Vgll3-deficient cells. Finally, overexpression of DAPK2 partially rescued autophagic activity and osteogenic differentiation in shVgll3 cells, supporting its role as a key downstream functional effector. FOXM1 was further implicated as a potential transcriptional regulator contributing to DAPK2 expression. Collectively, our findings suggest that VGLL3 may influence osteogenic differentiation in osteoblasts, potentially involving DAPK2-associated autophagy. - Source: PubMed
He YuhanWang ZiyiWeng YaoSitosari HeriatiZheng YilinQu YaxinIkegame MikaOkamura Hirohiko