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Western blot analysis of DGKθ on rat brain lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-DGKθ.
Immunofluorescent staining of SK-BR-3 cells.
BD Transduction Laboratories™ Purified Mouse Anti-DGKθ
BD Transduction Laboratories™ Purified Mouse Anti-DGKθ
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Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
The protein kinase C pathway is a major signal transduction system that is activated upon stimulation of transmembrane receptors by hormones, neurotransmitters, and growth factors. Key mediators in this pathway are increased intracellular free Ca2+ levels and formation of diacylglycerol (DAG). DGKθ (diacylglycerol kinase θ) restricts PKC activation through the phosphorylation of DAG molecules that contain an unsaturated fatty acid at the sn-2 position to produce phosphatidic acid (PA). DGKθ contains several regions that are found in signaling molecules where they function in lipid-protein and protein-protein interactions. A C-terminal catalytic domain, three CRDs (cysteine rich domains), a PH domain, and an N-terminal proline/glycine rich domain are structural features of DGKθ. Six potential PKC phosphorylation sites lie between CRD3 and the PH domain. Cell-specific expression differentiate multiple isoforms of DGK. DGKθ is expressed primarily within the cerebellar cortex and hippocampus of the brain, but is also found in the small intestine and liver. The presence of the RA (Ras-associating) domain suggests that DGKθ may mediate activity of the Ras-like small GTP binding proteins.
Development References (3)
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Bregoli L, Baldassare JJ, Raben DM. Nuclear diacylglycerol kinase-theta is activated in response to alpha-thrombin. J Biol Chem. 2001; 276(26):23288-23295. (Clone-specific: Immunofluorescence, Western blot). View Reference
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Houssa B, Schaap D, van der Wal J, et al. Cloning of a novel human diacylglycerol kinase (DGKtheta) containing three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain. J Biol Chem. 1997; 272(16):10422-10428. (Biology). View Reference
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Pilz A, Schaap D, Hunt D, Fitzgibbon J. Chromosomal localization of three mouse diacylglycerol kinase (DAGK) genes: genes sharing sequence homology to the Drosophila retinal degeneration A (rdgA) gene. Genomics. 1995; 26(3):599-601. (Biology). View Reference
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