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DYRK1B Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q9Y463
Clone Names 100617181
Additional Information
Gene ID 9149
Other Names Dual specificity tyrosine-phosphorylation-regulated kinase 1B, Minibrain-related kinase, Mirk protein kinase, DYRK1B, MIRK
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name DYRK1B
Synonyms MIRK
Function Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Plays an essential role in ribosomal DNA (rDNA) double-strand break repair and rDNA copy number maintenance (PubMed:33469661). During DNA damage, mediates transcription silencing in part via phosphorylating and enforcing DSB accumulation of the histone methyltransferase EHMT2 (PubMed:32611815). Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Inhibits the SHH and WNT1 pathways, thereby enhancing adipogenesis. In addition, promotes expression of the gluconeogenic enzyme glucose-6-phosphatase catalytic subunit 1 (G6PC1).
Cellular Location Nucleus. Nucleus, nucleolus. Chromosome. Note=Localizes to sites of double-strand breaks (DSBs) following DNA damage.
Tissue Location Highest expression in skeletal muscle, testis, heart and brain with little expression in colon or lung. Expressed in a variety of tumor cell lines.
Research Areas
Citations (0)
citation

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Background

DYRK1B is a member of the DYRK family of protein kinases.DYRK1B contains a bipartite nuclear localization signal and isfound mainly in muscle and testis. The protein is proposed to beinvolved in the regulation of nuclear functions. Three isoforms ofDYRK1B have been identified differing in the presence of twoalternatively spliced exons within the catalytic domain. [providedby RefSeq].

References

Lauth, M., et al. Nat. Struct. Mol. Biol. 17(6):718-725(2010)Yang, C., et al. Carcinogenesis 31(4):552-558(2010)Jin, K., et al. J. Biol. Chem. 284(34):22916-22925(2009)Deng, X., et al. Cancer Res. 69(8):3317-3324(2009)Janumyan, Y., et al. J. Biol. Chem. 283(49):34108-34120(2008)

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$ 277.78
Cat# BP16734c
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