Recombinant human DYRK3 protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant human DYRK3 protein is a Human Fragment protein, in the 63 to 568 aa range, expressed in Escherichia coli, with >70%, suitable for SDS-PAGE, WB, FuncS.
View Alternative Names
Dual specificity tyrosine-phosphorylation-regulated kinase 3, Regulatory erythroid kinase, REDK, DYRK3
- FuncS
Unknown
Functional Studies - Recombinant human DYRK3 protein (AB135222)
The specific activity of DYRK3 (ab135222) was determined to be 315 nmol/min/mg as per activity assay protocol and was equivalent to 240 nmol/min/mg as per radiometric assay
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human DYRK3 protein (AB135222)
SDS PAGE analysis of ab135222
- FuncS
Unknown
Functional Studies - Recombinant human DYRK3 protein (AB135222)
The specific activity of ab135222 was determined to be 242 nmol/min/mg.
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human DYRK3 protein (AB135222)
SDS-PAGE analysis of ab135222.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
General info
Function
Dual-specificity protein kinase that promotes disassembly of several types of membraneless organelles during mitosis, such as stress granules, nuclear speckles and pericentriolar material (PubMed : 29973724). Dual-specificity tyrosine-regulated kinases (DYRKs) autophosphorylate a critical tyrosine residue in their activation loop and phosphorylate their substrate on serine and threonine residues (PubMed : 29634919, PubMed : 9748265). Acts as a central dissolvase of membraneless organelles during the G2-to-M transition, after the nuclear-envelope breakdown : acts by mediating phosphorylation of multiple serine and threonine residues in unstructured domains of proteins, such as SRRM1 and PCM1 (PubMed : 29973724). Does not mediate disassembly of all membraneless organelles : disassembly of P-body and nucleolus is not regulated by DYRK3 (PubMed : 29973724). Dissolution of membraneless organelles at the onset of mitosis is also required to release mitotic regulators, such as ZNF207, from liquid-unmixed organelles where they are sequestered and keep them dissolved during mitosis (PubMed : 29973724). Regulates mTORC1 by mediating the dissolution of stress granules : during stressful conditions, DYRK3 partitions from the cytosol to the stress granule, together with mTORC1 components, which prevents mTORC1 signaling (PubMed : 23415227). When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol : acts by mediating the phosphorylation of the mTORC1 inhibitor AKT1S1, allowing full reactivation of mTORC1 signaling (PubMed : 23415227). Also acts as a negative regulator of EPO-dependent erythropoiesis : may place an upper limit on red cell production during stress erythropoiesis (PubMed : 10779429). Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells (PubMed : 10779429). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1 : this in turn inhibits p53/TP53 activity and apoptosis (PubMed : 20167603).
Sequence similarities
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.
Post-translational modifications
Ubiquitinated at anaphase by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome.. Protein kinase activity is activated following autophosphorylation at Tyr-369 (Probable). Autophosphorylation at Ser-350 stabilizes the protein and enhances the protein kinase activity (PubMed:9748265).
Subcellular localisation
Nucleus
Target data
Complementary Products
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com