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DYRK1A Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q13627 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 85584 Da |
| Antigen Region | 389-418 aa |
| Gene ID | 1859 |
|---|---|
| Other Names | Dual specificity tyrosine-phosphorylation-regulated kinase 1A, Dual specificity YAK1-related kinase, HP86, Protein kinase minibrain homolog, MNBH, hMNB, DYRK1A, DYRK, MNB, MNBH |
| Target/Specificity | This DYRK1A antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 389-418 amino acids from the Central region of human DYRK1A. |
| Dilution | WB~~1:2000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | DYRK1A Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | DYRK1A {ECO:0000303|PubMed:25620562, ECO:0000312|HGNC:HGNC:3091} |
|---|---|
| Function | Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities (PubMed:21127067, PubMed:8769099, PubMed:30773093, PubMed:20981014, PubMed:23665168). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3 (PubMed:23665168). Plays an important role in double- strand breaks (DSBs) repair following DNA damage (PubMed:31024071). Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR) (PubMed:30773093). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A (PubMed:25620562, PubMed:29849146). May play a role in a signaling pathway regulating nuclear functions of cell proliferation (PubMed:14500717). Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Has pro-survival function and negatively regulates the apoptotic process (By similarity). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1 (By similarity). This in turn inhibits p53/TP53 activity and apoptosis (By similarity). Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434' (By similarity). |
| Cellular Location | Nucleus. Nucleus speckle {ECO:0000250|UniProtKB:Q61214} |
| Tissue Location | Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
DYRK1A is a member of the Dual-specificity tyrosine phosphorylation-regulated kinase (DYRK) family. This member contains a nuclear targeting signal sequence, a protein kinase domain, a leucine zipper motif, and a highly conservative 13-consecutive-histidine repeat. It catalyzes its autophosphorylation on serine/threonine and tyrosine residues. It may play a significant role in a signaling pathway regulating cell proliferation and may be involved in brain development. This gene is a homolog of Drosophila mnb (minibrain) gene and rat Dyrk gene. It is localized in the Down syndrome critical region of chromosome 21, and is considered to be a strong candidate gene for learning defects associated with Down syndrome.
References
Adayev,T., Biochemistry 46 (25), 7614-7624 (2007)
Chang,H.S., Int. J. Cancer 120 (11), 2377-2385 (2007)
Alvarez,M., Mol. Biol. Cell 18 (4), 1167-1178 (2007)
Wissing,J., Mol. Cell Proteomics 6 (3), 537-547 (2007)
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