|Other Names||Serine/threonine-protein kinase DCLK2, CaMK-like CREB regulatory kinase 2, CL2, CLICK-II, CLICK2, Doublecortin domain-containing protein 3B, Doublecortin-like and CAM kinase-like 2, Doublecortin-like kinase 2, DCLK2, DCAMKL2, DCDC3B, DCK2|
|Target/Specificity||The synthetic peptide sequence is selected from aa 182-196 of HUMAN DCLK2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||DCAMKL2, DCDC3B, DCK2|
|Function||Protein kinase with a significantly reduced C(a2+)/CAM affinity and dependence compared to other members of the CaMK family. May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm (By similarity).|
|Cellular Location||Cytoplasm, cytoskeleton. Note=Colocalizes with microtubules.|
|Tissue Location||Expressed in the brain, heart and eyes.|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the protein kinase superfamily and the doublecortin family. The protein encoded by this gene contains two N-terminal doublecortin domains, which bind microtubules and regulate microtubule polymerization, a C-terminal serine/threonine protein kinase domain, which shows substantial homology to Ca2+/calmodulin-dependent protein kinase, and a serine/proline-rich domain in between the doublecortin and the protein kinase domains, which mediates multiple protein-protein interactions. The microtubule-polymerizing activity of the encoded protein is independent of its protein kinase activity. Mouse studies show that the DCX gene, another family member, and this gene share function in the establishment of hippocampal organization and that their absence results in a severe epileptic phenotype and lethality, as described in human patients with lissencephaly. Multiple alternatively spliced transcript variants have been identified.
Dijkmans, T.F., et al. Cent Nerv Syst Agents Med Chem 10(1):32-46(2010)
Kerjan, G., et al. Proc. Natl. Acad. Sci. U.S.A. 106(16):6766-6771(2009)
Gorelik, A., et al. Cell. Mol. Biol. Lett. 13(4):614-620(2008)
Tuy, F.P., et al. Dev. Neurosci. 30 (1-3), 171-186 (2008) :
Reiner, O., et al. BMC Genomics 7, 188 (2006) :
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