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Rabbit Anti-DYRK1B Recombinant Antibody (EG1015) (CBMAB-EN1198-LY)

The product is antibody recognizes DYR1B. The antibody EG1015 immunoassay techniques such as: WB: 1:500~1:1000 ELISA: 1:20000.
See all DYRK1B antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse
Clone
EG1015
Antibody Isotype
IgG
Application
WB: 1:500~1:1000 ELISA: 1:20000

Basic Information

Immunogen
The antibody was produced against synthesized peptide derived from internal of human DYR1B.
Specificity
Human, Mouse
Antibody Isotype
IgG
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!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Dual Specificity Tyrosine Phosphorylation Regulated Kinase 1B
Entrez Gene ID
Human9149
Mouse13549
UniProt ID
HumanQ9Y463
MouseQ9Z188
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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