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DAPK2 encodes a protein that belongs to the serine/threonine protein kinase family. Zusätzlich bieten wir Ihnen DAPK2 Antikörper (147) und viele weitere Produktgruppen zu diesem Protein an.
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miR (zeige MLXIP Proteine)-520h suppresses Death-associated protein kinase 2 (DAPK2) expression, as restoring DAPK2 abolished miR (zeige MLXIP Proteine)-520h-promoted drug resistance, and knockdown of DAPK2 mitigated cell death caused by the depletion of miR (zeige MLXIP Proteine)-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 (zeige AKT1 Proteine) and 14-3-3 (zeige YWHAQ Proteine) 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 (zeige CEBPA Proteine) during granulocytic differentiation but repressed by PML (zeige PML Proteine)-RARalpha (zeige RARA Proteine) in APL (zeige FASL Proteine).
DRP-1 (zeige CRMP1 Proteine) and ZIPk (zeige DAPK3 Proteine) most likely evolved from their ancient ancestor gene DAPk (zeige DAPK1 Proteine) 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 (zeige PRKG1 Proteine)-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