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MABN1848

Sigma-Aldrich

Anti-DYRK1A Antibody, clone 8D9

clone 8D9, from mouse

Synonym(s):

Dual specificity tyrosine-phosphorylation-regulated kinase 1A, Dual specificity YAK1-related kinase, MNBH, Protein kinase minibrain homolog, RP86

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

8D9, monoclonal

species reactivity

rat, mouse, human

species reactivity (predicted by homology)

chicken (based on 100% sequence homology)

technique(s)

western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

ambient

target post-translational modification

unmodified

Gene Information

chicken ... Dyrk1A(395233)
human ... DYRK1A(1859)
mouse ... Dyrk1A(13548)
rat ... Dyrk1A(25255)

General description

Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.2; UniProt Q63470; also known as Dual specificity YAK1-related kinase, MNBH, Protein kinase minibrain homolog, RP86) is encoded by the Dyrk1a (also known as Dyrk) gene (Gene ID 25255) in rat species. DYRK1A belongs to a family of conserved dual-specificity tyrosine-phosphorylated and regulated kinases (DYRKs) within the CMGC (CDK, MAPK, GSK, and CLK) group of eukaryote kinome. DYRK family members share a conserved kinase domain and an adjacent DYRK-homology domain or DH-box (DDDNXDY), wihile differing in their N- and C-terminal regions. DYRK1A is regulated by autophosphorylation on Ser, Thr and Tyr residues, but catalyzes phosphorylation of a broad-range of substrates only on Ser/Thr residues within the RPX(S/T)P motif with a preference for Pro at the +1 position (X). Known DYRK1A substrates include transcription factors (e.g. FKHR, CREB, Gli1, NFAT), splicing factors (e.g. cycling L2, SF3b/SAP155), glycogen synthase, as well as multiple proteins engaged in endocytosis in neurons, including dynamin and synaptojanin 1. DYRK1A is also implicated in promoting the formation of neurotoxic Aβ peptides by phosphorylating APP and presenilin-1. Human DYRK1A gene is located in the Down syndrome critical region of chromosome 21 and the protein plays an essential role in the development of the central nervous system. DYRK1A haploinsufficiency and mutations are the causes of intellectual disability (ID), microcephaly and dysmorphic features in human, while transgenic mice carrying extra copies of the gene exhibit learning defects and motor abnormalities.

Specificity

The specificity of target band detection was confirmed by antibody blocking with an excess amount of DYRK1A prior to Western blotting (Murakami, N., et al. (2009). Biochemistry. 48(39):9297-9305).

Immunogen

His-tagged recombinant rat DYRK1A N-terminal fragment.

Application

Anti-DYRK1A, clone 8D9, Cat. No. MABN1848, is a mouse monoclonal antibody that targets DYRK1A isoforms and has been tested in Western Blotting.
Immunohistochemistry Analysis: A 1:50-250 dilution from a representative lot detected nuclear DYRK1A immunoreactivity in human (prostate and pancreatic) cancer tissue and rat cerebral cortex tissue sections.

Western Blotting Analysis: A 1:500 dilution from a representative lot detected DYRK1A in 10 µg of HeLa cell lysate.

Western Blotting Analysis: A representative lot detected DYRK1A in NIH/3T3 cell lysate and human frontal cortex homogenates, as well as in DYRK1A and actin immunoprecipitates (Dowjat, K., et al. (2012). J. Neuropathol. Exp. Neurol. 71(12):1100-1112).

Western Blotting Analysis: A representative lot detected DYRK1A levels in lymphoblastoid cell lines (LCLs) from healthy control, Down syndrome (DS) and fragile X (FraX) human subjects (Dowjat, K., et al. (2012). J. Neuropathol. Exp. Neurol. 71(12):1100-1112).

Western Blotting Analysis: Representative lots detected DYRK1A in rat brain tissue homogenate and subfractionated extracts. The nuclear fraction had low DYRK1A, whereas the majority DYRK1A was found in the postnuclear fractions with clathrin-coated vesicles (CCVs) containing the highest level (Murakami, N., et al. (2012). PLoS One. 7(4):e34845; Murakami, N., et al. (2009). Biochemistry. 48(39):9297-9305).

Western Blotting Analysis: A representative lot detected recombinant rat DYRK1A-bound protein bands by a Western blotting-based DYRK1A overlay assay (Murakami, N., et al. (2009). Biochemistry. 48(39):9297-9305).

Western Blotting Analysis: A representative lot detected recombinant rat DYRK1A in GST-End1, but not GST-End2, pull-down. Clone 8D9 detected the C-terminal PEST domain deletion DYRK1A497 construct in the GST-amphiphysin SH3 domain (GST-Am-SH3) pull-down only in the presence of dynamin (Murakami, N., et al. (2009). Biochemistry. 48(39):9297-9305).
Research Category
Neuroscience

Quality

Evaluated by Western Blotting in HEK293 cell lysate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected DYRK1A in 10 µg of HEK293 cell lysate.

Target description

~90 kDa observed. 85.58/84.56/60.33/61.77/66.10 kDa (human isoform Long/1/2/3/4), 85.49 kDa (mouse), 85.54/84.51 kDa (rat isoform 1/2) calculated. Uncharacterized bands may be observed in some lysate(s).

Physical form

Format: Purified
Protein G purified.
Purified mouse IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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