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DAPK2 encodes a protein that belongs to the serine/threonine protein kinase family.
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Human Polyclonal DAPK2 Primary Antibody for IHC (p), WB - ABIN1882166
Satoh, Toyota, Itoh, Kikuchi, Obata, Sasaki, Suzuki, Yawata, Kusano, Fujita, Hosokawa, Yanagihara, Tokino, Imai: DNA methylation and histone deacetylation associated with silencing DAP kinase gene expression in colorectal and gastric cancers. in British journal of cancer 2002
Show all 7 Pubmed References
Human Polyclonal DAPK2 Primary Antibody for IHC (p), IHC - ABIN257703
Geering, Stoeckle, Rozman, Oberson, Benarafa, Simon: DAPK2 positively regulates motility of neutrophils and eosinophils in response to intermediary chemoattractants. in Journal of leukocyte biology 2014
Show all 2 Pubmed References
Human Polyclonal DAPK2 Primary Antibody for WB - ABIN4304244
Chen, Huang, Chu, Chen, Chou, Wang, Kulp, Teng, Wang, Chen: Energy restriction-mimetic agents induce apoptosis in prostate cancer cells in part through epigenetic activation of KLF6 tumor suppressor gene expression. in The Journal of biological chemistry 2011
This study suggests that miR (show MLXIP Antibodies)-520g contributes to tumor progression and drug resistance by post-transcriptionally downregulating DAPK2 in patients with epithelial ovarian cancer
Thyroid hormone (show PTH Antibodies) promotes selective autophagy via induction of DAPK2-SQSTM1 (show SQSTM1 Antibodies) cascade, which in turn protects hepatocytes from diethylnitrosamine-induced hepatotoxicity or carcinogenesis.
miR (show MLXIP Antibodies)-520h suppresses Death-associated protein kinase 2 (DAPK2) expression, as restoring DAPK2 abolished miR (show MLXIP Antibodies)-520h-promoted drug resistance, and knockdown of DAPK2 mitigated cell death caused by the depletion of miR (show MLXIP Antibodies)-520h.
that Death-associated protein kinase 2 effector functions are influenced by the protein's subcellular localization
This study links adipocyte expression of an autophagy-regulating kinase, lysosome-mediated clearance and fat cell lipid accumulation; it demonstrates obesity-related attenuated autophagy in adipocytes, and identifies DAPK2 dependence in this regulation.
DAPK2 is a novel kinase of mTORC1 and is a potential new member of this multiprotein complex, modulating mTORC1 activity and autophagy levels under stress and steady-state conditions.
DAPK2 regulates oxidative stress in cancer cells by preserving mitochondrial function
DAPK2-induced apoptosis is negatively regulated by Akt (show AKT1 Antibodies) and 14-3-3 (show YWHAQ Antibodies) proteins.
DAPK2 is upregulated in uterosacral ligaments in pelvic organ prolapse
The defect in chemotaxis in DAPK2-inactive granulocytes is likely a result of reduced polarization of the cells, mediated by a lack of MLC phosphorylation, resulting in radial F-actin and pseudopod formation.
DAPK2 is strongly and specifically expressed in interstitial cells of the cortex, providing a useful marker for this important cell population
These results suggest that DAPK2 is one of the targets of cGK (show PRKG1 Antibodies)-I in apoptosis induction.
The crystal and solution structures of murine DAPK2 were determined in the presence of the autoinhibitory domain, with and without bound nucleotides in the active site. Dimers of DAPK2 had a conformation that did not permit protein substrate binding.
DAPK2 was substantially up-modulated during late erythropoiesis
This gene encodes a protein that belongs to the serine/threonine protein kinase family. This protein contains a N-terminal protein kinase domain followed by a conserved calmodulin-binding domain with significant similarity to that of death-associated protein kinase 1 (DAPK1), a positive regulator of programmed cell death. Overexpression of this gene was shown to induce cell apoptosis. It uses multiple polyadenylation sites.
death-associated protein kinase 2
, DAP kinase 2
, DAP-kinase-related protein 1 beta isoform
, death-associated kinase 2