|Application ||WB, IHC-P, FC, E|
|Calculated MW||101155 Da|
|Antigen Region||912-942 aa|
|Other Names||Diacylglycerol kinase theta, DAG kinase theta, Diglyceride kinase theta, DGK-theta, DGKQ, DAGK4|
|Target/Specificity||This DGKQ antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 912-942 amino acids from the C-terminal region of human DGKQ.|
|Precautions||DGKQ Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor (By similarity). May be involved in cAMP- induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity.|
|Cellular Location||Cytoplasm. Cell membrane. Cytoplasm, cytoskeleton. Nucleus. Nucleus speckle. Note=Translocates to the nucleus in response to thrombin stimulation (PubMed:15632189). Translocates to the plasma membrane in response to steroid hormone receptor stimulation (PubMed:15632189). Translocation to the plasma membrane is dependent on G-protein coupled receptor stimulation and subsequent activation of PRKCE and probably PRKCH (PubMed:15632189)|
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Provided below are standard protocols that you may find useful for product applications.
Diacylglycerol (DAG) is an allosteric activator of protein kinase C. DAG also participates in regulating RAS and RHO family proteins by activating the guanine nucleotide exchange factors VAV and RASGRP1. DAG is also involved in the synthesis of phospholipids and triacylglycerols. Tight regulation of DAG levels is achieved via DAG kinases (DGKs), which remove DAG by phosphorylate it to phosphatidic acid.The predicted 882-amino acid human DGKQ (DGK-theta) protein is 90% identical in sequence to the rat homolog. DGK-theta is comprised of a pleckstrin homology domain and the conserved DGK putative catalytic domain. In contrast to other DGK isotypes, DGK-theta contains 3 rather than 2 cysteine-rich zinc-binding domains, an N-terminal proline- and glycine-rich region, and a RAS-associating domain. Highest tissue expression in the rat is in the brain. Defects in eye-specific DAGK genes cause retinal degeneration in Drosophila; thus, DAGK genes are candidates for human eye disease.
Pilz, A., et al., Genomics 26(3):599-601 (1995).
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