Anti-DYRK1A Antibody, clone 7F3

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. ~90 kDa doublet reported (Wegiel, J., et al. (2004). Brain Res. 1010(1-2):69-80).

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.

His-tagged recombinant rat DYRK1A N-terminal fragment (Wegiel, J., et al. (2004). Brain Res. 1010(1-2):69-80).

Anti-DYRK1A, clone 7F3, Cat. No. MABN1835, is a highly specific mouse monoclonal antibody that targets DYRK1A and has been tested in Immunocytochemistry, Immunofluorescence, Immunohistochemistry, and Western Blotting.

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected DYRK1A in rat thalamus tissue section.

Immunocytochemistry Analysis: A representative lot, pre-conjugated with Alexa Fluor^™ 568, immunostained the soma and processes of 2% formaldehyde-fixed, 0.05% saponin-permeabilized E-18 rat hippocampal neurons by fluorescent immunocytochemistry. DYRK1A immunoreactivity was more abundant in nuclei than in the cytoplasm. Co-localization of DYRK1A and clathrin heavy chain (CHC) immunoreactivity was very prominent in the processes and less significant in the soma (Murakami, N., et al. (2012). PLoS One. 7(4):e34845).

Immunofluorescence Analysis: A representative lot detected DYRK1A cellular localization in GFAP-positive astrocytes and in vimentin-positive endothelial cells by dual fluorescent immunohistochemistry staining of 10% formalin-fixed, PEG 1000-embeded human brain tissue sections (Wegiel, J., et al. (2004). Brain Res. 1010(1-2):69-80).

Immunohistochemistry Analysis: A representative lot detected DYRK1A immunoreactivity in paraffin-embedded fetal (20-week gestation) Down syndrome (DS) white matter associated with structures resembling the omnipresent cytoskeleton filamentous network in axons (Dowjat, K., et al. (2012). J. Neuropathol. Exp. Neurol. 71(12):1100-1112).

Immunohistochemistry Analysis: A representative lot detected age- and brain region-dependent DYRK1A immunoreactivity in 10% formalin-fixed, PEG 1000-embeded human brain tissue sections (Wegiel, J., et al. (2004). Brain Res. 1010(1-2):69-80).

Western Blotting Analysis: A representative lot detected both endogenous monkey DYRK1A and exogenously expressed full-length rat DYRK1A in COS-7 cells, as well as DYRK1A in human hippocampus tissue extracts. Antibody blocking with the immunogen prior to Western blotting abolished target band detection (Wegiel, J., et al. (2004). Brain Res. 1010(1-2):69-80).

Research Category
Neuroscience

The specificity of target band detection was confirmed by antibody blocking with the immunogen prior to Western blotting (Wegiel, J., et al. (2004). Brain Res. 1010(1-2):69-80).

Format: Purified

Protein G purified.

Purified mouse IgG2bκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

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

Evaluated by Immunohistochemistry in rat cerebellum tissue section.

Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected DYRK1A in rat cerebellum tissue section.

Concentration: Please refer to lot specific datasheet.

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