- 文献引用 : 9
|Application ||WB, IHC-P, E|
|Other Names||Dual specificity tyrosine-phosphorylation-regulated kinase 2, DYRK2|
|Target/Specificity||This DYRK2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 105-135 amino acids from the N-terminal region of human DYRK2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.|
|Storage||Maintain 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.|
|Precautions||DYRK2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
Author : Imawari Y1,2,Mimoto R2,Hirooka S3,Morikawa T2,Takeyama H2,Yoshida K1.
Cancer Sci. 2018 Feb;109(2):363-372. doi: 10.1111/cas.13459. Epub 2018 Jan 13.
Author : Mimoto R1,2, Imawari Y1,2, Hirooka S3, Takeyama H2, Yoshida K1.
Oncogene. 2016 Oct 10. doi: 10.1038/onc.2016.349. [Epub ahead of print]
Author : Moreno P1,2, Lara-Chica M1, Soler-Torronteras R1, Caro T3, Medina M3, Álvarez A2, Salvatierra Á2, Muñoz E1, Calzado MA1.
PLoS One. 2015 Nov 18;10(11):e0143376. doi: 10.1371/journal.pone.0143376. eCollection 2015.
Author : Nomura S1, Suzuki Y2, Takahashi R3, Terasaki M4, Kimata R5, Terasaki Y6, Hamasaki T7, Kimura G8, Shimizu A9, Kondo Y10.
BMC Urol. 2015 Jun 19;15:53. doi: 10.1186/s12894-015-0040-7.
Author : Enomoto Y1, Yamashita SI, Yoshinaga Y, Fukami Y, Miyahara S, Nabeshima K, Iwasaki A.
Tumour Biol. 2014 Aug 6. [Epub ahead of print]
Author : PÃ©rez M, GarcÃa-Limones C, Zapico I, Marina A, Schmitz ML, MuÃ±oz E, Calzado MA.
J Mol Cell Biol. 2012 Oct;4(5):316-30. doi: 10.1093/jmcb/mjs047. Epub 2012 Aug 9.
Author : Taira N, Mimoto R, Kurata M, Yamaguchi T, Kitagawa M, Miki Y, Yoshida K.
J Clin Invest. 2012 Mar 1;122(3):859-72. doi: 10.1172/JCI60818. Epub 2012 Feb 6.
Author : Yamashita S, Chujo M, Tokuishi K, Anami K, Miyawaki M, Yamamoto S, Kawahara K.
J Thorac Cardiovasc Surg. 2009 Dec;138(6):1303-8. doi: 10.1016/j.jtcvs.2009.08.003. Epub 2009 Oct 9.
Author : Yamashita S, Chujo M, Moroga T, Anami K, Tokuishi K, Miyawaki M, Kawano Y, Takeno S, Yamamoto S, Kawahara K.
Anticancer Res. 2009 Jul;29(7):2753-7.
Provided below are standard protocols that you may find useful for product applications.
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.
Becker, W., et al., J. Biol. Chem. 273(40):25893-25902 (1998).