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Dyrk2 blocking peptide

Mouse Dyrk2 Antibody (C-term) Blocking peptide

Gene Names
Dyrk2; 1810038L18Rik
Synonyms
Dyrk2; Mouse Dyrk2 Antibody (C-term) Blocking peptide; Dual specificity tyrosine-phosphorylation-regulated kinase 2; Dyrk2 blocking peptide
Ordering
Specificity
The synthetic peptide sequence used to generate the antibody was selected from the C-term region of Mouse Dyrk2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Form/Format
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
Sequence Length
599
Cellular Location
Cytoplasm. Nucleus. Note: Translocates into the nucleus following DNA damage.
Preparation and Storage
Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.
Related Product Information for Dyrk2 blocking peptide
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. 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) (By similarity). Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
UniProt Accession #
Molecular Weight
66,556 Da
NCBI Official Full Name
Dual specificity tyrosine-phosphorylation-regulated kinase 2
NCBI Official Synonym Full Names
dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2
NCBI Official Symbol
Dyrk2
NCBI Official Synonym Symbols
1810038L18Rik
NCBI Protein Information
dual specificity tyrosine-phosphorylation-regulated kinase 2
UniProt Protein Name
Dual specificity tyrosine-phosphorylation-regulated kinase 2
UniProt Gene Name
Dyrk2
UniProt Entry Name
DYRK2_MOUSE

Uniprot Description

DYRK2: a dual-specificity protein kinase of the DYRK family. Localizes in the cytoplasm. Phosphorylates the translation initiation factor eIF2B at Ser539, priming it for phosphorylation by glycogen synthase kinase-3.

Protein type: Protein kinase, CMGC; Kinase, protein; Protein kinase, dual-specificity (non-receptor); EC 2.7.12.1; CMGC group; DYRK family; Dyrk2 subfamily

Cellular Component: cytoplasm; nucleoplasm; nucleus; ribonucleoprotein complex; ubiquitin ligase complex

Molecular Function: ATP binding; magnesium ion binding; manganese ion binding; protein serine/threonine kinase activity; protein-tyrosine kinase activity; ubiquitin binding

Biological Process: DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; negative regulation of NFAT protein import into nucleus; peptidyl-tyrosine phosphorylation; positive regulation of glycogen biosynthetic process; protein amino acid phosphorylation; smoothened signaling pathway

Research Articles on Dyrk2

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Product Notes

The Dyrk2 dyrk2 (Catalog #AAA9220434) is a Blocking Peptide and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Dyrk2, Blocking Peptide" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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