Background: Dyrk, the vertebrate of Drosophilia minibrain, is a dual-specificity kinase predominately expressed in the central nervous system. The human clone has been isolated from the Downs' syndrome critical region and it is potentially implicated in the neuropathology of the disease. Main features of the protein include an N-terminal nuclear translocation signal, a putative leucine zipper domain, a core kinase domain with some similarity to kinases involved in cell cycle regulation and a C-terminal PEST sequence. The Dyrk kinase can be phosphorylated on tyrosine residues, leading to an active kinase that can phosphorylated itself or exogenous substrates on both tyrosine and serine/threonine residues. Dyrk can also multimerize and translocate to the nucleus. Present studies on Dyrk suggest a potential role for this kinase in the exit from the cell cycle and the beginning of neuronal differentiation.
Positive Control: Expressed in a variety of embryonic and adult tissues. Expressed abundantly in neurons of the brain, spinal cord, and retina in developing embryos.
Purification Method: Ammonium Sulfate Precipitation.
Source: Sheep were immunized with a recombinant protein corresponding to amino acids 486 to 763 of the mouse Dyrk1A protein.
References: 1. Kentrup, H., et al., Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII. J. Biol. Chem. 1996, 271, 3488-3495.
2. Song, W.-J., et al., Isolation of human and murine homologues of the Drosophilia minibrain gene: Human homologue maps to 21q22.2 in the Down syndrome critical region. Genomics 1996, 38, 331-339.
3. Becker, W. & Joost, H.G. Structural and functional characteristics of Dyrk, a novel subfamily of protein kinases with dual specificity. Prog. Nucleic Acid Res. Mol. Biol. 1999, 62, 1-17.
UniProt: Q61214.
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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