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Mouse Anti-DYRK1B Recombinant Antibody (2E8) (CBMAB-D2021-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Dual Specificity Tyrosine Phosphorylation Regulated Kinase 1B (DYRK1B). The antibody can be used for immunoassay techniques, such as ELISA, IF, WB.
See all DYRK1B antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
2E8
Antibody Isotype
IgG2a, κ
Application
ELISA, IF, WB

Basic Information

Immunogen
DYRK1B (AAH25291, 479 a.a. ~ 569 a.a) partial recombinant protein with GST tag. The immunogen sequence: DNRTYRYSNR YCGGPGPPIT DCEMNSPQVP PSQPLRPWAG GDVPHKTHQA PASASSLPGT GAQLPPQPRY LGRPPSPTSP PPPELMDVSL V
Specificity
Human
Antibody Isotype
IgG2a, κ
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.
Epitope
aa 479-569

Target

Full Name
Dual Specificity Tyrosine Phosphorylation Regulated Kinase 1B
Introduction
DYRK1B belongs to a family of nuclear-localized protein kinases. The encoded protein participates in the regulation of the cell cycle. Expression of this gene may be altered in tumor cells, and mutations in this gene were found to cause abdominal obesity-metabolic syndrome 3.
Entrez Gene ID
9149
UniProt ID
Q9Y463
Alternative Names
Dual Specificity Tyrosine Phosphorylation Regulated Kinase 1B; Minibrain-Related Kinase; Dual Specificity Tyrosine-(Y)-Phosphorylation Regulated Kinase 1B; Mirk Protein Kinase; MIRK; Dual-Specificity Tyrosine-(Y)-Phosphorylation Regulated Kinase 1B;
Research Area
Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. 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).
Biological Process
Adipose tissue development Source: UniProtKB
Myoblast fusion Source: Ensembl
Peptidyl-serine phosphorylation Source: GO_Central
Peptidyl-threonine phosphorylation Source: GO_Central
Positive regulation of transcription, DNA-templated Source: UniProtKB
Protein autophosphorylation Source: InterPro
Protein phosphorylation Source: UniProtKB
Cellular Location
Nucleus
Involvement in disease
Abdominal obesity-metabolic syndrome 3 (AOMS3):
A form of abdominal obesity-metabolic syndrome, a disorder characterized by abdominal obesity, high triglycerides, low levels of high density lipoprotein cholesterol, high blood pressure, and elevated fasting glucose levels. AOMS3 is characterized by early-onset coronary artery disease, central obesity, hypertension, and diabetes.
PTM
Autophosphorylated on tyrosine residues. Phosphorylated by MAP kinase. Tyrosine phosphorylation may be required for dimerization.

Bhat, N., Narayanan, A., Fathzadeh, M., Kahn, M., Zhang, D., Goedeke, L., ... & Mani, A. (2022). Dyrk1b promotes hepatic lipogenesis by bypassing canonical insulin signaling and directly activating mTORC2 in mice. The Journal of Clinical Investigation, 132(3).

Zhuang, L., Jia, K., Chen, C., Li, Z., Zhao, J., Hu, J., ... & Yan, X. (2022). DYRK1B-STAT3 drives cardiac hypertrophy and heart failure by impairing mitochondrial bioenergetics. Circulation, 145(11), 829-846.

Bhat, N., Narayanan, A., Fathzadeh, M., Shah, K., Dianatpour, M., Abou Ziki, M. D., & Mani, A. (2022). Dyrk1b promotes autophagy during skeletal muscle differentiation by upregulating 4e-bp1. Cellular Signalling, 90, 110186.

Papenfuss, M., Lützow, S., Wilms, G., Babendreyer, A., Flaßhoff, M., Kunick, C., & Becker, W. (2022). Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B. Scientific reports, 12(1), 1-15.

Lee Walmsley, D., Murray, J. B., Dokurno, P., Massey, A. J., Benwell, K., Fiumana, A., ... & Hubbard, R. E. (2021). Fragment-derived selective inhibitors of dual-specificity kinases DYRK1A and DYRK1B. Journal of Medicinal Chemistry, 64(13), 8971-8991.

Dong, C., An, L., Yu, C. H., & Huen, M. S. (2021). A DYRK1B-dependent pathway suppresses rDNA transcription in response to DNA damage. Nucleic acids research, 49(3), 1485-1496.

Chang, C. C., Chiu, C. C., Liu, P. F., Wu, C. H., Tseng, Y. C., Lee, C. H., & Shu, C. W. (2021). Kinome-Wide siRNA Screening Identifies DYRK1B as a Potential Therapeutic Target for Triple-Negative Breast Cancer Cells. Cancers, 13(22), 5779.

Dong, C., West, K. L., Tan, X. Y., Li, J., Ishibashi, T., Yu, C. H., ... & Huen, M. S. (2020). Screen identifies DYRK1B network as mediator of transcription repression on damaged chromatin. Proceedings of the National Academy of Sciences, 117(29), 17019-17030.

Yousefelahiyeh, M., Xu, J., Alvarado, E., Yu, Y., Salven, D., & Nissen, R. M. (2018). DCAF7/WDR68 is required for normal levels of DYRK1A and DYRK1B. PloS one, 13(11), e0207779.

Becker, W. (2018). A wake‐up call to quiescent cancer cells–potential use of DYRK 1B inhibitors in cancer therapy. The FEBS Journal, 285(7), 1203-1211.

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

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