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DYRK2 Antibody

Mouse Monoclonal Antibody (Mab)

     
  • 1 - DYRK2 Antibody AM2060b
    DYRK2 Antibody (Cat. #AM2060b) western blot analysis in A549 cell line lysates (35μg/lane).This demonstrates the DYRK2 antibody detected the DYRK2 protein (arrow).
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q92630
Other Accession NP_003574.1
Reactivity Human
Host Mouse
Clonality Monoclonal
Isotype IgG1
Clone Names 492CT4.2.4
Calculated MW 66652 Da
Additional info
Gene ID 8445
Other Names Dual specificity tyrosine-phosphorylation-regulated kinase 2, DYRK2
Target/Specificity This DYRK2 antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 105-135 amino acids from human DYRK2.
Dilution WB~~1:100~500
Format Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsDYRK2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name DYRK2
Function Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser- 641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro).
Cellular Location Cytoplasm. Nucleus. Note=Translocates into the nucleus following DNA damage
Tissue Location Testis, after the onset of spermatogenesis.
Research Areas

BACKGROUND

DYRK2 belongs to a family of protein kinases whose members are presumed to be involved in cellular growth and/or development. The family is defined by structural similarity of their kinase domains and their capability to autophosphorylate on tyrosine residues. DYRK2 has demonstrated tyrosine autophosphorylation and catalyzed phosphorylation of histones H3 and H2B in vitro. Two isoforms of DYRK2 have been isolated. The predominant isoform, isoform 1, lacks a 5' terminal insert.

REFERENCES

Taira, N., et al. J. Biol. Chem. 285(7):4909-4919(2010)
Yamashita, S., et al. J. Thorac. Cardiovasc. Surg. 138(6):1303-1308(2009)
Yamashita, S., et al. Anticancer Res. 29(7):2753-2757(2009)
Maddika, S., et al. Nat. Cell Biol. 11(4):409-419(2009)
Rikova, K., et al. Cell 131(6):1190-1203(2007)

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