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Facts about Diacylglycerol kinase zeta.
Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (By similarity). Activates PIP5K1A action via generation of phosphatidic acid (PubMed:15157668).
Human | |
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Gene Name: | DGKZ |
Uniprot: | Q13574 |
Entrez: | 8525 |
Belongs to: |
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eukaryotic diacylglycerol kinase family |
DAGK5; DAGK6DAG kinase zeta; DGKZ; DGKzeta; DGK-zeta; diacylglycerol kinase zeta; diacylglycerol kinase, zeta 104kDa; diacylglycerol kinase, zeta; Diglyceride kinase zeta; EC 2.7.1.107; hDGKzeta
Mass (kDA):
124.128 kDA
Human | |
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Location: | 11p11.2 |
Sequence: | 11; NC_000011.10 (46332905..46380554) |
Highest levels in brain, and substantial levels in skeletal muscle, heart, and pancreas. Isoform 1 is predominantly expressed in muscle.
Cytoplasm. Nucleus. Cell membrane. Cell projection, lamellipodium.
Diacylglycerol Kinase zeta plays a critical role in the intracellular signaling cascade. Boster supplies high-affinity primary antibodies against its receptors. This enzyme also inhibits proteinkinase C and regulates intracellular signaling. Scientists from all over the globe can submit results with this product in order to receive product credit.
Boster is the best choice for high-affinity, specific antibody detections of the DGKZ marker. Its products are extensively tested against positive and negative samples. These antibodies have been widely utilized in the research community, and are trusted for being reliable. For example, the Boster antibody was validated against human esophageal stellate cells.
Boster Bio's DGKZ antibody is part the Picoband(tm). The BosterBio Anti-DGKZ/DGK–zeta Antibody reacts in the following ways: Human, Mouse, Rat The BosterBio antibody can be used in a variety of samples. Its high affinity has been confirmed by quantitative tests using untransfected and recombinant cell lines.
DGKZ, which is diacylglycerol kinase or DGKZ. This enzyme reduces the activity protein kinase. Mice without this enzyme display abnormal lithium-sensitive behavior.
Using a baculovirus/insect cell expression method, DGKz was isolated from insect cells. It was easily purified to near homogeneity. It is catalytically enough for crystal screening. However, its enzymatic parameters are different from other DGK isozymes. These differences have a profound impact on the development of new therapeutics for diseases and conditions involving DGK.
The phosphorylation of DGKZ is mediated by a phosphatase called Yamaguchi Y. Yamaguchi Y phosphorylates DGK-zeta at the Ser-22 and Ser-26 of its pleckstrin homology domain. In vivo, phosphorylation of the MARCKS homology domain reduced DGK-zeta nuclear accumulation. These findings suggest a mechanism for controlling mitogenic signals' activity by regulating intracellular DGK zeta localization.
Although DGKZ is located in the nucleus and hippocampal neurons of the brain, it is not yet known what its function is. Although the binding mechanism is not known, it is believed to be involved in leptin receptor signaling. It is abundant in the hippocampus and moderately abundant in the dentate gyrus, retina, and cortex. Its binding motif, which is found in the caudate and thalmus and controls presynaptic discharge during long term potentiation, is also present.
Purification of DGKz-FL allows detailed analysis of the DGKZ enzyme. Purification will enable you to identify disease-related roles for this enzyme and develop targeted therapies. It plays an important role within immune regulation. It has been proven that it inhibits the activation of T-cells and prevents inflammatory response. Further studies of DGKZ on human patients will aid in the development vaccines and other treatments for symptoms.
Diacylglycerol kinase-Z (DGKZ) has recently been linked to several diseases, including diabetic cardiomyopathy. This enzyme is an endogenous regulator of PKC activity and is involved in the downstream insulin signaling pathway. PKCbeta is a PKC-beta kinase inhibitor that prevents insulin-stimulated Akt phosphorylation.
TLR signaling can be enhanced by DGKZ’s role in regulating TLR mediated innate immunopathy. Moreover, DGKZ prevents activation of PKC alpha by blocking the activity JNK. This is important for anti-inflammatory immunity. DGKZ also inhibits activation TLRs. This in turn enhances the anti-inflammatory immune response.
Using SILAC Phosphoproteomics DGKZ can easily be identified in tissue and cell expression data. It can also be associated with microRNAs via nonconserved miRNA seed sequences. If DGKZ expression is high in tissue samples than in other tissues, this indicates that it is highly expressed. This suggests that DGKZ could be associated with many types and types of cancer.
A protein called DGKZ, which is important in osteosarcoma cell growth, acts as an MYC interactor and inhibits the MYC/ERK1/2 pathway. This protein is likely to play multiple roles in osteosarcoma development and oncogenesis. Inhibiting its expression could affect the disease's proliferative abilities.
This protein is overexpressed in osteosarcoma tissues. In vitro studies found that DGKZ knockdown in osteosarcoma cells inhibited proliferation, and that knockdown in MYC-dependent genes impaired expression. Xenografts from DGKZ-silencing mice had smaller tumors than those in the control group. Microarray and IPA analyses also revealed a significant alternation of osteosarcoma cells, and the MYC pathway was identified as a downstream target for DGKZ.
The eukaryotic eacylglycerol kinase kinase DGKZ family includes the DGKZ gene. It may mediate activation of phospholipases. However, it may also regulate activity of protein kinase E.
This protein also has antitumor benefits. It was shown to suppress osteosarcoma tumorigenesis by nude mice in one study. Moreover DGKZ silencing significantly reduced osteosarcoma xenograft size. In addition, DGKZ inhibits bioluminescent signals and suppresses tumor growth.
Using a lentiviral vector expressing a DGKZ gene fused with 3 x FLAG tag sequence, we knocked down DGKZ expression in OS cells. We used a non-targeting sequence, pGCSIL–GFP, to verify the effectiveness of this strategy. The HOS cells were then plated at 4x105 cell per well. Specific antibodies were used for the subsequent infection. The DGKZ FLAG compound was then isolated using specific antibodies.
After removing anti-FLAG, we immunoprecipitated each protein with the corresponding ligand, 3x FLAG. After that, the samples were separated using SDS-PAGE. Then, they were transferred onto a PVDF membrane. The membranes were blocked with 5% non-fat milk, followed by a secondary antibody conjugated to horseradish peroxidase. Finally, we exposed the membranes the ECL systems and measured the absorbance. The Boster bio DGKZ regulates intracellular signals in ovarian cancer cells.
PMID: 8626588 by Bunting M., et al. Molecular cloning and characterization of a novel human diacylglycerol kinase zeta.
PMID: 9159104 by Ding L., et al. Alternative splicing of the human diacylglycerol kinase zeta gene in muscle.