DYRK1B Antibody detects endogenous levels of total DYRK1B protein. This antibody detects the three major alternative splicing variants reported for DYRK1B.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxyl terminus of human DYRK1B. Antibodies were purified by protein affintiy chromatography.
Background
The DYRK family includes several dual-specificity tyrosine-phosphorylated and regulated kinases capable of phosphorylating proteins at both tyrosine and serine/threonine residues (1). The DYRK family was identified based on homology to the yeast Yak1 (2) and the Drosophila minibrain (mnb) kinases (3). Seven mammalian isoforms have been discovered, including DYRK1A, DYRK1B, DYRK1C, DYRK2, DYRK3, DYRK4, and DYRK4B. Differences in substrate specificity, expression, and subcellular localization are seen across the DYRK family (4,5). All DYRK proteins have a Tyr-X-Tyr motif in the catalytic domain activation loop, with phosphorylation of the second Tyr residue (e.g. Tyr312 of DYRK1A) necessary for kinase activity. DYRKs typically autophosphorylate the tyrosine residue within their activation loop, but phosphorylate substrates at serine and threonine residues (1,6).In contrast to the ubiquitous DYRK1A, DYRK1B exhibits relatively restricted expression with highest levels found in the testis and muscle (7,8). Three major DYRK1B splice variants demonstrate distinct expression patterns and functional properties (9). DYRK1B plays a critical role in myoblast differentiation by affecting cell motility, transcription, cell cycle progression and survival (10,11). In addition, DYRK1B contributes to the survival of certain cancer cells (7,12,13).
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