Recombinant Human DYRK4 Kinase was resolved with SDS-PAGE under reducing (Lane 1) and non-reducing (Lane 2) conditions.
The activity of DYRK4 is based on the MSA technology, and the content and ratio of the substrate and the product are directly separated and detected in real time and dynamically by the different migration rates of the substrate and the product after the enzymatic reaction.
DYRK4 is a member of the conserved dual-specific tyrosine phosphorylation-regulated kinase (DYRK) family, which contains five members (DYRK1A, DYRK1B, DYRK2, DYRK3, and DYRK4) and has a conserved N-terminal DYRK homology cassette (DH) and an adjacent kinase domain. It has a highly conserved Tyr-X-Tyr amino acid motif in the catalytic domain of the activation loop, and phosphorylation of the second tyrosine residue is essential for full activation of DYRKs, with mature DYRKs phosphorylating only serine or threonine residues on the substrate. In contrast to other DYRKs, little is known about the function of DYRK4, and no substrate has been identified for this kinase. It has been reported that mouse and rat Dyrk4 is a testis-specific kinase predominantly expressed in the testis. However, Dyrk4-deficient mice are fertile, which may be redundant in terms of function because DYRKs are strongly expressed in the testis.
