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DYRK2 Antibody
Primary Antibodies

DYRK2 Antibody #8143

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Citations (3)

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# Product Name Application Reactivity
  • WB
H M R Hm Mk

Supporting Data

MW (kDa) 66, 60

Application Key:

  • W-Western
  • IP-Immunoprecipitation
  • IHC-Immunohistochemistry
  • ChIP-Chromatin Immunoprecipitation
  • IF-Immunofluorescence
  • F-Flow Cytometry
  • E-P-ELISA-Peptide

Species Cross-Reactivity Key:

  • H-Human
  • M-Mouse
  • R-Rat
  • Hm-Hamster
  • Mk-Monkey
  • Mi-Mink
  • C-Chicken
  • Dm-D. melanogaster
  • X-Xenopus
  • Z-Zebrafish
  • B-Bovine
  • Dg-Dog
  • Pg-Pig
  • Sc-S. cerevisiae
  • Ce-C. elegans
  • Hr-Horse
  • All-All Species Expected


Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

DYRK2 Antibody recognizes endogenous levels of total DYRK2 protein. This antibody recognizes both the 66 and 60 kDa splice variants.

Species predicted to react based on 100% sequence homology:

Bovine, Dog, Pig

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly545 of human DYRK2 protein. Antibodies are purified by protein A and peptide affinity chromatography.


The DYRK family includes several dual-specificity tyrosine-phosphorylated and regulated kinases capable of phosphorylating proteins at both Tyr and Ser/Thr 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; phosphorylation of the second Tyr residue (e.g. Tyr312 of DYRK1A) is necessary for kinase activity. DYRKs typically autophosphorylate the Tyr residue within their activation loop, but phosphorylate substrates at Ser and Thr residues (1,6).

DYRK2 is thought to play a role in checkpoint control of the cell cycle. DYRK2 can phosphorylate p53 at Ser46 following cellular damage, leading to activation of the apoptotic response (7). Overexpression of DYRK2 has also been reported in esophageal and lung adenocarcinomas (8), and its expression levels were shown to be predictive of chemotherapy treatment outcomes in non-small cell lung cancer (9).

  1. Becker, W. and Joost, H.G. (1999) Prog. Nucleic Acid Res. Mol. Biol. 62, 1-17.
  2. Garrett, S. and Broach, J. (1989) Genes Dev. 3, 1336-1348.
  3. Tejedor, F. et al. (1995) Neuron 14, 287-301.
  4. Kentrup, H. et al. (1996) J. Biol. Chem. 271, 3488-3495.
  5. Becker, W. et al. (1998) J. Biol. Chem. 273, 25893-25902.
  6. Lochhead, P.A. et al. (2005) Cell 121, 925-936.
  7. Taira N et al. (2007) Mol Cell 25, 725–38
  8. Miller, C.T. et al. (2003) Cancer Res 63, 4136-43.
  9. Yamashita, S. et al. (2009) Anticancer Res 29, 2753-7.

Pathways & Proteins

Explore pathways + proteins related to this product.

For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

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