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The authors show that IFT88 interacts with DGKdelta, and is associated with COPII-coated vesicles at the the endoplasmic reticulum exit sites.
results suggest that DGKdelta controls the down-regulation of cyclin D1 expression by attenuating the PKC signaling pathway for C2C12 myogenic differentiation
the amount of 5-HT in the cerebral cortex was significantly decreased in DGKdelta-KO mice. These data strongly suggest that OCD-like behaviors in the DGKdelta-KO mice are caused by comprehensive and composite serotonergic hypofunction.
Results strongly suggest that a deficiency of Diacylglycerol kinase delta induces obsessive-compulsive disorder-like behavior through enhancing axon/neurite outgrowth in the brain.
DGKdelta deficiency impairs AMPK signaling and lipid metabolism, thereby highlighting the deleterious role of excessive lipid metabolites in the development of peripheral insulin resistance and type 2 diabetes pathogenesis.
DGKD preferably metabolizes palmitic acid-containing diacylglycerol species supplied from the PC-PLC pathway.
DGKdelta markedly increases lipid synthesis, at least in part as a result of promoting the synthesis of fatty acids.
These results suggest that DGKzeta is involved in IQGAP1/Rac1-mediated phagocytosis upon LPS stimulation in macrophages.
Results suggest that diacylglycerol kinase delta regulates epidermal growth factor receptors by modulating protein kinase C signaling.
Metabolic flexibility, evident by the transition between lipid and carbohydrate utilization during fasted and fed conditions, was impaired in DGKdelta haploinsufficient mice.
purification and characterization of DGKepsilon's enzymatic and conformational properties
Diacylglycerol signaling limits Akt activation through diacylglycerol kinase delta and PHLPP2.
This study demonistrated that the lack of association of DGKD SNPs with PD in the Han Chinese population.
Zinc site mutations impair DGKdelta localization to cytoplasmic puncta and enhance localization the plasma membrane.
Data indicate a novel mechanism where diacylglycerol kinase delta and protein kinase Calpha modulate the levels of ubiquitinated epidermal growth factor receptors through Akt and ubiquitin-specific protease 8.
Alternative splicing of the gene generates two isoforms differing in their expression patterns and in regulatory functions
Phosphorylation is involved in the control of subcellular localization of DGKdelta1.
Disruption of diacylglycerol kinase delta (DGKD) is associated with seizures in humans and mice.
Study identified reduced diacylglycerol kinase delta (DGKdelta) expression and DGK activity in skeletal muscle from type 2 diabetic patients.
Polymerization of DGK delta regulates the activity of the enzyme by sequestering DGK delta in an inactive cellular location.
This gene encodes a cytoplasmic enzyme that phosphorylates diacylglycerol to produce phosphatidic acid. Diacylglycerol and phosphatidic acid are two lipids that act as second messengers in signaling cascades. Their cellular concentrations are regulated by the encoded protein, and so it is thought to play an important role in cellular signal transduction. Alternative splicing results in two transcript variants encoding different isoforms.
diacylglycerol kinase, delta 130kDa
, diacylglycerol kinase delta-like
, DAG kinase delta
, diacylglycerol kinase delta
, diglyceride kinase delta