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Mouse Anti-DYRK2 Recombinant Antibody (CBYCD-466) (CBMAB-D2023-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Dual Specificity Tyrosine Phosphorylation Regulated Kinase 2 (DYRK2). The antibody can be used for immunoassay techniques, such as WB, IHC.
See all DYRK2 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Rat
Clone
CBYCD-466
Antibody Isotype
IgG2b
Application
WB, IHC

Basic Information

Immunogen
E. coli-derived recombinant human DYRK2, a.a. 1-107, Accession # NP_003574
Specificity
Human, Rat
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Dual Specificity Tyrosine Phosphorylation Regulated Kinase 2
Introduction
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.
Entrez Gene ID
Human8445
Rat314862
UniProt ID
HumanQ92630
RatF1LYY7
Alternative Names
Dual Specificity Tyrosine Phosphorylation Regulated Kinase 2; EC 2.7.12.1; Dual-Specificity Tyrosine-(Y)-Phosphorylation Regulated Kinase 2; Dual Specificity Tyrosine-(Y)-Phosphorylation Regulated Kinase 2; EC 2.7.12;
Research Area
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).
Biological Process
Cellular response to DNA damage stimulus Source: UniProtKB
Intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
Negative regulation of calcineurin-NFAT signaling cascade Source: UniProtKB
Peptidyl-serine phosphorylation Source: GO_Central
Peptidyl-threonine phosphorylation Source: GO_Central
Positive regulation of glycogen biosynthetic process Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Regulation of signal transduction by p53 class mediator Source: Reactome
Smoothened signaling pathway Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm. Translocates into the nucleus following DNA damage.
PTM
Autophosphorylates cotranslationally on the second tyrosine residue in the Tyr-X-Tyr motif in the activation loop, but once mature, does not have any protein tyrosine kinase activity. Phosphorylated at Thr-106 and Ser-442 by ATM in response to genotoxic stress.
Under normal conditions, polyubiquitinated in the nucleus by MDM2, leading to its proteasomal degradation. Phosphorylation on Thr-106 and Ser-442 by ATM in response to genotoxic stress disrupts MDM2 binding and prevents MDM2-mediated ubiquitination and subsequent proteasomal degradation. Polyubiquitinated by SIAH2, leading to its proteasomal degradation. Polyubiquitinated by SIAH2 oCcurs under normal conditions, and is enhanced in response to hypoxia.

Lara-Chica, M., Correa-Sáez, A., Jiménez-Izquierdo, R., Garrido-Rodríguez, M., Ponce, F. J., Moreno, R., ... & Calzado, M. A. (2022). A novel CDC25A/DYRK2 regulatory switch modulates cell cycle and survival. Cell Death & Differentiation, 29(1), 105-117.

Kawamura, A., Yoshida, S., Aoki, K., Shimoyama, Y., Yamada, K., & Yoshida, K. (2022). DYRK2 maintains genome stability via neddylation of cullins in response to DNA damage. Journal of Cell Science, 135(11), jcs259514.

Tandon, V., de la Vega, L., & Banerjee, S. (2021). Emerging roles of DYRK2 in cancer. Journal of Biological Chemistry, 296.

Moreno, R., Banerjee, S., Jackson, A. W., Quinn, J., Baillie, G., Dixon, J. E., ... & de la Vega, L. (2021). The stress-responsive kinase DYRK2 activates heat shock factor 1 promoting resistance to proteotoxic stress. Cell Death & Differentiation, 28(5), 1563-1578.

Correa-Sáez, A., Jiménez-Izquierdo, R., Garrido-Rodríguez, M., Morrugares, R., Muñoz, E., & Calzado, M. A. (2020). Updating dual-specificity tyrosine-phosphorylation-regulated kinase 2 (DYRK2): molecular basis, functions and role in diseases. Cellular and Molecular Life Sciences, 77(23), 4747-4763.

Yoshida, S., Aoki, K., Fujiwara, K., Nakakura, T., Kawamura, A., Yamada, K., ... & Yoshida, K. (2020). The novel ciliogenesis regulator DYRK2 governs Hedgehog signaling during mouse embryogenesis. Elife, 9, e57381.

Kumamoto, T., Yamada, K., Yoshida, S., Aoki, K., Hirooka, S., Eto, K., ... & Yoshida, K. (2020). Impairment of DYRK2 by DNMT1‑mediated transcription augments carcinogenesis in human colorectal cancer. International Journal of Oncology, 56(6), 1529-1539.

Yoshida, S., & Yoshida, K. (2019). Multiple functions of DYRK2 in cancer and tissue development. FEBS letters, 593(21), 2953-2965.

Park, C. S., Lewis, A. H., Chen, T. J., Bridges, C. S., Shen, Y., Suppipat, K., ... & Lacorazza, H. D. (2019). A KLF4-DYRK2–mediated pathway regulating self-renewal in CML stem cells. Blood, 134(22), 1960-1972.

Yokoyama-Mashima, S., Yogosawa, S., Kanegae, Y., Hirooka, S., Yoshida, S., Horiuchi, T., ... & Yoshida, K. (2019). Forced expression of DYRK2 exerts anti-tumor effects via apoptotic induction in liver cancer. Cancer letters, 451, 100-109.

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For research use only. Not intended for any clinical use.

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