|Other Names||Dual specificity protein kinase CLK2, CDC-like kinase 2, CLK2|
|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.|
|Function||Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.|
|Cellular Location||Isoform 1: Nucleus. Nucleus speckle. Note=Inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.|
|Tissue Location||Endothelial cells.|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the CLK family of dualspecificity protein kinases. CLK family members have been shown tointeract with, and phosphorylate, serine- and arginine-rich (SR)proteins of the spliceosomal complex, which is a part of theregulatory mechanism that enables the SR proteins to control RNAsplicing. Note that this gene is distinct from TELO2 gene(GeneID:9894), which shares CLK2 and hCLK2 symbol aliases in commonwith this gene, but encodes a protein that is involved in telomerelength regulation.
Nam, S.Y., et al. J. Biol. Chem. 285(41):31157-31163(2010)Eisenreich, A., et al. Circ. Res. 104(5):589-599(2009)Rendtlew Danielsen, J.M., et al. J. Biol. Chem. 284(7):4140-4147(2009)Castle, J.C., et al. Nat. Genet. 40(12):1416-1425(2008)Jin, J., et al. Curr. Biol. 14(16):1436-1450(2004)
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