Recombinant human DGKZ/DGK-zeta protein (Active) is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095, PubMed:9159104). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095, PubMed:9159104). Also plays an important role in the biosynthesis of complex lipids (Probable). Does not exhibit an acyl chain-dependent substrate specificity among diacylglycerol species (PubMed:19744926, PubMed:22108654, PubMed:9159104). Can also phosphorylate 1-alkyl-2-acylglycerol in vitro but less efficiently and with a preference for alkylacylglycerols containing an arachidonoyl group (PubMed:15544348, PubMed:19744926, PubMed:22627129). The biological processes it is involved in include T cell activation since it negatively regulates T-cell receptor signaling which is in part mediated by diacylglycerol (By similarity). By generating phosphatidic acid, stimulates PIP5KIA activity which regulates actin polymerization (PubMed:15157668). Through the same mechanism could also positively regulate insulin-induced translocation of SLC2A4 to the cell membrane (By similarity). Isoform 1. Regulates RASGRP1 activity. Isoform 2. Does not regulate RASGRP1 activity.
DAGK6, DGKZ, Diacylglycerol kinase zeta, DAG kinase zeta, Diglyceride kinase zeta, DGK-zeta
Recombinant human DGKZ/DGK-zeta protein (Active) is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS.
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF
Affinity purified.
Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095, PubMed:9159104). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095, PubMed:9159104). Also plays an important role in the biosynthesis of complex lipids (Probable). Does not exhibit an acyl chain-dependent substrate specificity among diacylglycerol species (PubMed:19744926, PubMed:22108654, PubMed:9159104). Can also phosphorylate 1-alkyl-2-acylglycerol in vitro but less efficiently and with a preference for alkylacylglycerols containing an arachidonoyl group (PubMed:15544348, PubMed:19744926, PubMed:22627129). The biological processes it is involved in include T cell activation since it negatively regulates T-cell receptor signaling which is in part mediated by diacylglycerol (By similarity). By generating phosphatidic acid, stimulates PIP5KIA activity which regulates actin polymerization (PubMed:15157668). Through the same mechanism could also positively regulate insulin-induced translocation of SLC2A4 to the cell membrane (By similarity).
Belongs to the eukaryotic diacylglycerol kinase family.
Phosphorylation of the MARCKS homology domain by PKC reduces nuclear accumulation of DGK-zeta.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
DGKZ also known as DGK-zeta or DGKζ is an enzyme that belongs to the diacylglycerol kinase family and plays an important role in lipid signaling pathways. The 'zeta' isoform of DGK sometimes noted in scientific literature as DGK ART and DGK MEXICO catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) by ATP-dependent phosphorylation impacting signal transduction. DGKZ has a molecular mass of approximately 115 kDa. It shows expression in various tissues including brain heart and skeletal muscle with higher expression levels typically seen in the nervous system where it affects neurotransmitter signaling.
DGKZ influences cellular processes such as growth differentiation and apoptosis by regulating DAG and PA levels. It forms part of a complex network of proteins involved in intracellular signaling cascades exerting effects on protein kinase C (PKC) activity. The regulatory function of DGKZ within cellular activity highlights its role in maintaining normal cellular homeostasis and responding to extracellular signals. Its enzymatic activity influences DAG-mediated pathways which are important for the activation and deactivation of downstream signaling proteins.
DGKZ plays a critical role within the signaling pathways such as the phosphoinositide signaling and mTOR pathways. It serves as an important modulator of lipid signaling within the diacylglycerol- and phosphatidic acid-mediated signaling pathways impacting protein interactions and signaling mechanisms. Other proteins related through these pathways include PKC and mTOR with which DGKZ interacts to modulate functions such as cell proliferation and survival. The enzymatic conversion of DAG to PA by DGKZ actively regulates the availability of these lipid signaling molecules and therefore modulates their downstream effects.
DGKZ has associations with neurological disorders and cancer. Abnormal regulation or expression of DGKZ contributes to pathologies such as Alzheimer's disease where impaired lipid signaling affects neuronal function and survival. Additionally its dysregulation may promote cancer progression through aberrant cell signaling pathways. DGKZ interacts with proteins like PKC which play a role in these diseases making it a potential therapeutic target. Understanding its function and interactions helps offer insights into the development of targeted therapies for these conditions.
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The specific activity of ab268445 was 18.2 nmol/min/mg in a kinase assay using Dilauroyl-sn-glycerol as substrate.
SDS-PAGE analysis of ab268445.
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