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DAPK2 encodes a protein that belongs to the serine/threonine protein kinase family. Additionally we are shipping DAPK2 Antibodies (147) and many more products for this protein.
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miR (show MLXIP Proteins)-520h suppresses Death-associated protein kinase 2 (DAPK2) expression, as restoring DAPK2 abolished miR (show MLXIP Proteins)-520h-promoted drug resistance, and knockdown of DAPK2 mitigated cell death caused by the depletion of miR (show MLXIP Proteins)-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 Proteins) and 14-3-3 (show YWHAQ Proteins) 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.
The tumor suppressor gene DAPK2 is induced by the myeloid transcription factors PU.1 and C/EBPalpha (show CEBPA Proteins) during granulocytic differentiation but repressed by PML (show PML Proteins)-RARalpha (show RARA Proteins) in APL (show FASL Proteins).
DRP-1 (show CRMP1 Proteins) and ZIPk (show DAPK3 Proteins) most likely evolved from their ancient ancestor gene DAPk (show DAPK1 Proteins) by two gene duplication events that occurred close to the emergence of vertebrates
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 Proteins)-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