|Other Names||Dual specificity protein kinase CLK3, CDC-like kinase 3, CLK3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7531a was selected from the N-term region of human CLK3 . 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. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.|
|Cellular Location||Isoform 1: Nucleus. Cytoplasm. Cytoplasmic vesicle, secretory vesicle, acrosome|
|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 protein belonging to the serine/threonine type protein kinase family. This protein is a nuclear dual-specificity kinase that regulates the intranuclear distribution of the serine/arginine-rich (SR) family of splicing factors. Alternatively spliced transcript variants have been described for this gene, but their biological validity has not been determined. Pseudogenes located on chromosomes 1 and 9 have been found for this gene.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Hanes, J., et al., J. Mol. Biol. 244(5):665-672 (1994).
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