|Other Names||Dual specificity protein kinase CLK2, CDC-like kinase 2, CLK2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7530a was selected from the N-term region of human CLK2 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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 dual specificity protein kinases. CLK family members have shown to interact with, and phosphorylate, serine- and arginine-rich (SR) proteins of the spliceosomal complex, which is a part of the regulatory mechanism that enables the SR proteins to control RNA splicing. This protein kinase is involved in the regulation of several cellular processes and may serve as a link between cell cycle progression, apoptosis, and telomere length regulation.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Winfield, S.L., et al., Genome Res. 7(10):1020-1026 (1997).Lee, K., et al., J. Biol. Chem. 271(44):27299-27303 (1996).Hanes, J., et al., J. Mol. Biol. 244(5):665-672 (1994).
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