|Other Names||Dual specificity protein kinase CLK1, CDC-like kinase 1, CLK1, CLK|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7529a was selected from the N-term region of human CLK1 . 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 and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA.|
|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 CDC2-like (or LAMMER) family of dual specificity protein kinases. In the nucleus, the encoded protein phosphorylates serine/arginine-rich proteins involved in pre-mRNA processing, releasing them into the nucleoplasm. The choice of splice sites during pre-mRNA processing may be regulated by the concentration of transacting factors, including serine/arginine rich proteins. Therefore, the encoded protein may play an indirect role in governing splice site selection.
Prasad, J., et al., Mol. Cell. Biol. 23(12):4139-4149 (2003).Talmadge, C.B., et al., Hum. Genet. 103(4):523-524 (1998).Hanes, J., et al., J. Mol. Biol. 244(5):665-672 (1994).Johnson, K.W., et al., J. Biol. Chem. 266(6):3402-3407 (1991).Ben-David, Y., et al., EMBO J. 10(2):317-325 (1991).
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