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DYRK1A protein, human

DYRK1A (Dual-Specificity Tyrosine Phosphorylation-Regulated Kinase 1A) is a protein kinase that plays a crucial role in various cellular processes, including cell cycle regulation, neuronal development, and signal transduction.
This protein is expressed in the nucleus and cytoplasm, and its dysregulation has been implicated in the pathogenesis of several neurological disorders, such as Alzheimer's disease and Down syndrome.
DYRK1A is an important target for therapeutic interventions, and the PubCompare.ai platform can help researchers identify the most effective products and protocols for studying this protein, enhancing reproducibility and accuracy in their reasearch.

Most cited protocols related to «DYRK1A protein, human»

1
Structural Determination of DYRK Kinases
Cited 10 times
All diffraction data were indexed and integrated using MOSFLM (Leslie and Powell, 2007 ) and scaled using SCALA (Evans, 2006 (link)). All models were refined with REFMAC5 (Murshudov et al., 2011 (link)).
The DYRK1A structure was solved by molecular replacement using Phaser (McCoy et al., 2007 (link)) and a search ensemble of the coordinates from two CLK kinases (PDB ID codes 2EXE and 1Z57). Four molecules were present in the asymmetric unit and, after NCS averaging and density modification in dm (Cowtan, 1994 ), the resulting phases could be utilized in ARP/wARP (Langer et al., 2008 (link)) to autobuild the main parts of one of the molecules in the asymmetric unit. After further model building in Coot (Emsley et al., 2010 (link)), this molecule was used to generate the other three molecules for restrained refinement with tight NCS restraints. Rebuilding and refinement (including TLS parameters) resulted in the final model.
The DYRK1A peptide complex and the DYRK2 structure were both solved by molecular replacement using Phaser, with the structure of the inhibitor-bound DYRK1A as a search molecule.
Soundararajan M., Roos A.K., Savitsky P., Filippakopoulos P., Kettenbach A.N., Olsen J.V., Gerber S.A., Eswaran J., Knapp S, & Elkins J.M. (2013). Structures of Down Syndrome Kinases, DYRKs, Reveal Mechanisms of Kinase Activation and Substrate Recognition. Structure(London, England:1993), 21(6), 986-996.
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Publication 2013
Clk dual-specificity kinases DYRK1A protein, human Peptides
2
DYRK1A Kinase Structural Characterization
Cited 6 times
Recombinant DYRK1A was purified
as previously described60 (link) and was treated
with TEV protease to remove the N-terminal His6 tag. The
kinase at ∼13–15 mg/mL in 50 mM HEPES, pH 7.5, 500 mM
NaCl and 5 mM DTT was incubated with the inhibitors at 1 mM prior
to crystallization. Crystals were obtained using the sitting drop
vapor diffusion method at 4 °C using either 2 M ammonium sulfate,
0.2 M Na/K tartrate, 0.1 M citrate, pH 5.6 (for 5s and 5t), or 37% PEG 400, 0.2 M lithium sulfate, 0.1 M Tris, pH
8.8 (for 5j), as the reservoir solutions. Diffraction
data collected at Diamond Light Source, beamline I04-1, were processed
with XDS71 (link) or mosflm72 (link) and subsequently scaled with Scala from CCP4 suite.73 (link) Structures were determined by molecular replacement
method using Phaser74 (link) and the coordinates
of DYRK1A structure60 (link) as a search model.
Iterative cycles of manual model building in COOT75 (link) alternated with refinement using Refmac,76 (link) and a TLS model calculated from TLSMD server77 (link) was performed. The geometric correctness of
the final model was verified with MolProbity.78 (link) Data collection and refinement statistics are summarized in Table 3. DYRK1A-ligand complexes (pdb id): DYRK1A-5j (4YLJ); DYRK1A-5s (4YLK); DYRK1A-5t (4YLL).
Falke H., Chaikuad A., Becker A., Loaëc N., Lozach O., Abu Jhaisha S., Becker W., Jones P.G., Preu L., Baumann K., Knapp S., Meijer L, & Kunick C. (2015). 10-Iodo-11H-indolo[3,2-c]quinoline-6-carboxylic Acids Are Selective Inhibitors of DYRK1A. Journal of Medicinal Chemistry, 58(7), 3131-3143.
Publication 2015
Citrates Crystallization Diamond Diffusion DYRK1A protein, human HEPES his6 tag inhibitors Ligands Light lithium sulfate polyethylene glycol 400 Sulfate, Ammonium Tartrates TEV protease Tromethamine
3
Clinical Assessment of DYRK1A Mutations
Cited 5 times
We performed a detailed clinical assessment of all eight patients with sporadic DYRK1A mutations, including the five new patients described here as well as three individuals with ASD for whom there was previously only limited clinical information available.7 (link) Additionally we assessed a ninth patient whose variant was determined to not likely lead to DYRK1A loss of function. Patients underwent a thorough assessment, including physical exam, dysmorphological assessment, a review of medical history, and comprehensive neurocognitive and diagnostic battery. The battery included clinician observation and parent reporting across domains of cognition, memory, language, motor, executive functioning, social, repetitive and atypical behaviors, and adaptive ability. In addition, psychiatric presentation was evaluated and gold standard ASD assessments (Autism Diagnostic Observation Schedule (ADOS), Autism Diagnostic Interview - Revised, clinical judgment) were completed for patients where possible.
van Bon B.W., Coe B.P., Bernier R., Green C., Gerdts J., Witherspoon K., Kleefstra T., Willemsen M.H., Kumar R., Bosco P., Fichera M., Li D., Amaral D., Cristofoli F., Peeters H., Haan E., Romano C., Mefford H.C., Scheffer I., Gecz J., de Vries B.B, & Eichler E.E. (2015). Disruptive de novo mutations of DYRK1A lead to a syndromic form of autism and ID. Molecular psychiatry, 21(1), 126-132.
Publication 2015
Acclimatization Autistic Disorder Clinical Reasoning Cognition Diagnosis DYRK1A protein, human Gold Memory Mutation Parent Patients Physical Examination
4
Targeted XIST expression in hiPSC
Cited 5 times
The DS iPSC line was cultured in 10 μM of Rho-associated protein kinases (ROCK) inhibitor (Calbiochem; Y27632) 24 h before electroporation. Single cells (1×107) were harvested using TryPLE select (Invitrogen), resuspended in 1 x PBS and electroporated with a total of 55 μg DNA including five plasmids (XIST, DYRK1A ZFN1, DYRK1A ZFN2, rtTA/puro, and AAVS1 ZFN) with both 3:1 and 5:1 ratios of XIST: rtTA/puro. The electroporation conditions were 220v, and 750 μF (BioRad Gene Pulser II System). Cells were subsequently plated on puromycin-resistant DR4 MEF feeders (Open Biosystems, Cat#: MES3948) in hiPSC medium supplemented with ROCK inhibitor for the first 24 h. Over 300 colonies remained after 12 days of 0.4 μg/ml puromycin selection and 245 randomly chosen individual colonies across 36 pooled wells were examined by interphase DNA/RNA FISH for the presence and expression of XIST, correct targeting and retention of trisomy (since some subclones lacked XIST or showed just two DYRK1A DNA signals). Over 100 individual clones were isolated and characterized, and those of interest, containing targeted XIST on one of three DYRK1A loci, were frozen. Six single target clones with good pluripotent morphology, OCT4 positive staining, correct targeting to one trisomic chromosome, and good XIST RNA paint were expanded for further characterization. One double and one triple target line, two non-target clones, and one disomic clone were also isolated and frozen. Targeting and correct chromosome number (47) was confirmed by interphase and metaphase FISH and genome integrity by high resolution G-band karyotype and CGH array.
Jiang J., Jing Y., Cost G.J., Chiang J.C., Kolpa H.J., Cotton A.M., Carone D.M., Carone B.R., Shivak D.A., Guschin D.Y., Pearl J.R., Rebar E.J., Byron M., Gregory P.D., Brown C.J., Urnov F.D., Hall L.L, & Lawrence J.B. (2013). Translating Dosage Compensation to Trisomy 21. Nature, 500(7462), 296-300.
Publication 2013
Cells Chromosomes Clone Cells DYRK1A protein, human Electroporation Fishes Freezing Genitalia Genome Human Induced Pluripotent Stem Cells Induced Pluripotent Stem Cells Interphase Karyotype Metaphase Plasmids POU5F1 protein, human Proteins Puromycin Retention (Psychology) rho-Associated Kinases Trisomy Y 27632
5
Targeted XIST expression in hiPSC
Cited 5 times
The DS iPSC line was cultured in 10 μM of Rho-associated protein kinases (ROCK) inhibitor (Calbiochem; Y27632) 24 h before electroporation. Single cells (1×107) were harvested using TryPLE select (Invitrogen), resuspended in 1 x PBS and electroporated with a total of 55 μg DNA including five plasmids (XIST, DYRK1A ZFN1, DYRK1A ZFN2, rtTA/puro, and AAVS1 ZFN) with both 3:1 and 5:1 ratios of XIST: rtTA/puro. The electroporation conditions were 220v, and 750 μF (BioRad Gene Pulser II System). Cells were subsequently plated on puromycin-resistant DR4 MEF feeders (Open Biosystems, Cat#: MES3948) in hiPSC medium supplemented with ROCK inhibitor for the first 24 h. Over 300 colonies remained after 12 days of 0.4 μg/ml puromycin selection and 245 randomly chosen individual colonies across 36 pooled wells were examined by interphase DNA/RNA FISH for the presence and expression of XIST, correct targeting and retention of trisomy (since some subclones lacked XIST or showed just two DYRK1A DNA signals). Over 100 individual clones were isolated and characterized, and those of interest, containing targeted XIST on one of three DYRK1A loci, were frozen. Six single target clones with good pluripotent morphology, OCT4 positive staining, correct targeting to one trisomic chromosome, and good XIST RNA paint were expanded for further characterization. One double and one triple target line, two non-target clones, and one disomic clone were also isolated and frozen. Targeting and correct chromosome number (47) was confirmed by interphase and metaphase FISH and genome integrity by high resolution G-band karyotype and CGH array.
Jiang J., Jing Y., Cost G.J., Chiang J.C., Kolpa H.J., Cotton A.M., Carone D.M., Carone B.R., Shivak D.A., Guschin D.Y., Pearl J.R., Rebar E.J., Byron M., Gregory P.D., Brown C.J., Urnov F.D., Hall L.L, & Lawrence J.B. (2013). Translating Dosage Compensation to Trisomy 21. Nature, 500(7462), 296-300.
Publication 2013
Cells Chromosomes Clone Cells DYRK1A protein, human Electroporation Fishes Freezing Genitalia Genome Human Induced Pluripotent Stem Cells Induced Pluripotent Stem Cells Interphase Karyotype Metaphase Plasmids POU5F1 protein, human Proteins Puromycin Retention (Psychology) rho-Associated Kinases Trisomy Y 27632

Most recents protocols related to «DYRK1A protein, human»

1
Colocalization Analysis for Trait Associations
Colocalization analysis takes into account five hypotheses: H0 (no association between the locus and either trait), H1 (locus has an association with first trait only), H2 (locus has an association with second trait only), H3 (locus has an association with both traits but driven by different SNPs which are not in linkage disequilibrium (LD)), H4 (locus has an association with both traits driven by same SNPs). For Project 3: Colocalization pipeline, we considered colocalization analysis with a posterior probability of colocalization in H4 (PPH4) greater than 0.8 to be significant. We utilized the coloc R package21 ,22 (link) and summary statistics from ref. 7 (link). We used eQTL data from a cerebellar cortical meta-analysis of four cohorts23 (link), publicly available from the AMP-AD Knowledge Portal24 . As an example for our pipeline, we extracted the region ± 500 kb around DYRK1A, nominated in Nalls et al. 2019, from the GWAS summary statistics and eQTL data. To visualize the results, we employed the eQTpLot R package25 (link), which can generate different plots for GWAS and eQTL signal colocalization, as well as the correlation between their p values and enrichment of eQTLs among variants and LD of loci of interest, allowing efficient and intuitive visualization of gene expression and trait interaction. We used our previously generated results for DYRK1A and whole brain eQTL as an example for creating visualizations using this package. (Fig. 3a).Results from the downstream analysis of genetic variation projects.

a Displays the locus of interest, in this case, ±500 kb from DYRK1A, and the horizontal line depicts the GWAS significance threshold of P = 5 × 10–8. Displays the genes in the locus of interest. b Depicts the Leiden gene networks and correlations for significant eQTLs for PD controls and PD cases. c Depicts the general workflow for the variant interaction pipeline.

Leonard H.L., Murtadha R., Martinez-Carrasco A., Jama A., Müller-Nedebock A.C., Gil-Martinez A.L., Illarionova A., Moore A., Bustos B.I., Jadhav B., Huxford B., Storm C., Towns C., Vitale D., Chetty D., Yu E., Grenn F.P., Salazar G., Rateau G., Iwaki H., Elsayed I., Foote I.F., Jansen van Rensburg Z., Kim J.J., Yuan J., Lake J., Brolin K., Senkevich K., Wu L., Tan M.M., Periñán M.T., Makarious M.B., Ta M., Pillay N.S., Betancor O.L., Reyes-Pérez P.R., Alvarez Jerez P., Saini P., al-Ouran R., Sivakumar R., Real R., Reynolds R.H., Hu R., Abrahams S., Rao S.C., Antar T., Leal T.P., Iankova V., Scotton W.J., Song Y., Singleton A., Nalls M.A., Dey S., Bandres-Ciga S., Blauwendraat C, & Noyce A.J. (2023). The IPDGC/GP2 Hackathon - an open science event for training in data science, genomics, and collaboration using Parkinson’s disease data. NPJ Parkinson's Disease, 9, 33.
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Publication 2023
Brain Cortex, Cerebellar DYRK1A protein, human Gene Expression Gene Regulatory Networks Genes Genetic Diversity Genome-Wide Association Study Single Nucleotide Polymorphism
2
Molecular Dynamics of Cytochrome P450 and DYRK1A
The 3D crystal structure of human Cytochrome P450 1A2 (CYP1A2, PDB ID: 2HI4), Dual specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A, PDB ID: 7A4O), Dual specificity tyrosine-phosphorylation-regulated kinase 1B (DYRK1B, PDB ID: 7A4O), and Dual specificity protein kinase (CLK1, PDB ID: 1Z57) proteins were retrieved by a research collaborator from the structural bioinformatics protein data bank (RCSB-PDB) (https://www.rcsb.org/ accessed on 28 July 2022). The molecular interaction of BP with the predicted target proteins was carried out using AutoDock Tools 4.0 [60 (link)]. Input files such as pdbqt of both the BP and target proteins, grid parameter, and docking parameter were prepared as previously described using AutoDock [61 (link)]. BP with a minimum binding energy (ΔG) towards the target proteins during the post-docking analysis was considered for a further molecular simulation analysis [62 (link)]. Molecular dynamic simulations of 100,000 picoseconds (ps) were performed to examine the flexibility and stability of the analog BP with CYP1A2 and DYRK1A enzymes at 300 K using the Groningen Machine for Chemical Simulations (GROMACS 5.1.2) package [63 (link)]. System preparation, system equilibration, and post-equilibration procedures were performed as stated in the Methods in Supplementary Materials. Analyses of the root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), and Radius of gyration (Rg) between the protein and BP in each frame were accomplished using the GROMACS command utilities.
Haridevamuthu B., Manjunathan T., Wilson Alphonse C.R., Kumar R.S., Thanigaivel S., Chandra Kishore S., Sundaram V., Gopinath P., Arockiaraj J, & Bellucci S. (2023). Functionalized Sulfur-Containing Heterocyclic Analogs Induce Sub-G1 Arrest and Apoptotic Cell Death of Laryngeal Carcinoma In Vitro. Molecules, 28(4), 1856.
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Publication 2023
CYP1A2 protein, human dual-specificity tyrosine-phosphorylation regulated kinase 1B DYRK1A protein, human Enzymes Homo sapiens Plant Roots Post Technique Protein Kinases Proteins Protein Targeting, Cellular Radius Reading Frames
3
Western Blot Analysis of NFAT and DYRK1A
Total protein in each sample was extracted using RIPA lysis buffer (Beyotime Biotechnology). The protein concentration was determined using the BCA protein concentration quantification kit (Beyotime Biotechnology). Denatured proteins were separated using 5× SDS-PAGE and transferred to PVDF membranes followed by blocking with 5% nonfat dry milk in Tris-buffered saline with 0.05% Tween 20 and probed with primary antibodies overnight at 4℃. Following washing, membranes were incubated with goat peroxidase-conjugated secondary antibodies at 37℃ for 2 hours. The reactions were detected using the Pierce ECL Western Blotting Substrate (Thermo Fisher). The bands were visualized via exposure to an x-ray beam in a dark room and semi-quantified analyzed using Tanon Image software. The ratio of the densitometric values of NFATc1, phosphorylated NFATc1, or DYRK1A bands to those of β-actin bands were used to determine relative expression. The primary and secondary antibodies included: mouse anti-β-actin (43 kDa, 1:1,000 dilution; Santa Cruz), mouse anti-NFATc1 (110,140 kDa, 1:500; Wanleibi), rabbit anti-NFATc1-P (phospho S237, 110, 140 kDa, 1:1,000; Abcam), rabbit anti-DYRK1A (46, 60, 86 kDa, 1:1,000; Abcam), Peroxidase Affini Pure Donkey Anti-Mouse IgG (H+L, 1:5,000; Jackson), and Peroxidase Affini Pure Goat Anti-Rabbit IgG (H+L, 1:10,000; Jackson).
Qi S.S., Miao Y., Sheng Y.Y., Hu R.M., Zhao J, & Yang Q.P. (2023). MicroRNA-1246 Inhibits NFATc1 Phosphorylation and Regulates T Helper 17 Cell Activation in the Pathogenesis of Severe Alopecia Areata. Annals of Dermatology, 35(1), 46-55.
Publication 2023
Actins anti-IgG Antibodies Buffers Densitometry DYRK1A protein, human Equus asinus Goat Milk, Cow's Mus Peroxidase polyvinylidene fluoride Proteins Rabbits Radiography Radioimmunoprecipitation Assay Saline Solution SDS-PAGE Technique, Dilution Tissue, Membrane Tween 20
4
Extraction and Analysis of RNA from Mouse Cortex
RNA was obtained from cortical tissue of Ts2Cje and Eu mice treated with vehicle or the KYCCSRK peptide. Tissues were lysed with an appropriate volume of QIAzol Reagent (QIAzol Lysis Reagent, Qiagen, Hilden, Germany). Subsequently, chloroform was added (1:5, Sigma-Aldrich, St. Louis, MO, USA), and samples were kept for 3 min at RT before being centrifuged at 12,000 rpm and 4 °C for 15 min. Following that, isopropanol (100%, Sigma-Aldrich, St. Louis, MO, USA) was added to each sample at RT for 10 min to separate RNA. Then, samples were centrifuged at 12,000 rpm and 4 °C for 15 min. The supernatant was discarded, and pellets were washed with 75% ethanol (Sigma-Aldrich, St. Louis, MO, USA) followed by further centrifugation at 7500 rpm and 4 °C for 5 min. The pellets were resuspended in RNAse-free H2O (Sigma-Aldrich, St. Louis, MO, USA). The RNA was quantified using the Biospec Nano reverse transcribed using the cDNA High-Capacity kit (Applied Biosystems, Foster City, CA, USA), including reverse transcriptase, random primers, and buffer according to the manufacturer’s instructions. The cDNA was produced through a series of heating and annealing cycles in the MultiGene OPTIMAX 96-well Thermocycler (LabNet International, Edison, NJ, USA). Real-time PCR was carried out using the SensiFAST™ SYBR® and No-ROX Kit (Bioline, London, UK) in a CFX Connect Real-Time PCR machine (Bio-Rad Laboratories, Hercules, CA, USA). Primers used for the RT-PCR are DYRK1A FW: 5′-TGGGGCAGAGGATATACCAGT-3′ and RV: 5′- GTCGATAGCAAGGTCATAAGGCA-3′ and BACE1 FW 5′-GGATTATGGTGGCCTGAGCA-3′ RV 5′-CACGAGAGGAGACGACGATG-3′ (BACE1: NM_011792.7; DYRK!A: NM_007890.2).
Tramutola A., Lanzillotta S., Aceto G., Pagnotta S., Ruffolo G., Cifelli P., Marini F., Ripoli C., Palma E., Grassi C., Di Domenico F., Perluigi M, & Barone E. (2023). Intranasal Administration of KYCCSRK Peptide Rescues Brain Insulin Signaling Activation and Reduces Alzheimer’s Disease-like Neuropathology in a Mouse Model for Down Syndrome. Antioxidants, 12(1), 111.
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Publication 2023
BACE1 protein, human Buffers Centrifugation Chloroform DNA, Complementary DYRK1A protein, human Endoribonucleases Ethanol Isopropyl Alcohol Kidney Cortex Mice, House Oligonucleotide Primers Optimax Pellets, Drug Peptides Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction RNA-Directed DNA Polymerase Tissues
5
Exploring Key Genes and Pathways in Co-DEmiRNA Network
We obtained all the network's key node genes with statistical significance, including ZNF460, FBN1, CDK6, BTG2, CBX6, DYRK1A, and so on. We obtained some significant pathways corresponding to hub genes (Fig. 5). The figure shows that the PI3K/AKT signaling pathway was the most enriched KEGG pathway. In addition, GO-BP analysis reveals that Ras protein signal transduction and extracellular structure organization are the most enriched biological process. GO-CC analysis revealed that the enriched cellular components were collagen-containing extracellular matrix, cell leading edge, ruffle, and other parts. GO-MF analysis revealed that protein serine/threonine kinase activity, extracellular matrix structural constituents, and growth factor binding were the top enriched molecular functions.

KEGG pathway and GO enrichment analysis of Hub genes related to Co-DEmiRNAs. The stronger the correlation between miRNAs and pathways, the larger the number of counts and the larger the bubbles (The p value is determined by color. The closer the color is to red, the smaller the P value. P < 0.05 considered statistically significant)

Li Z., Fu R., Wen X, & Zhang L. (2023). Network analysis reveals miRNA crosstalk between periodontitis and oral squamous cell carcinoma. BMC Oral Health, 23, 19.
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Publication 2023
Biological Processes CDK6 protein, human Cellular Structures Collagen DYRK1A protein, human Extracellular Matrix Fibrillin-1 Genes Growth Factor MicroRNAs Morphogenesis Phosphatidylinositol 3-Kinases Protein-Serine-Threonine Kinases ras Proteins Signal Transduction Signal Transduction Pathways

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Dyrk1a by Cell Signaling Technology
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DYRK1A is a dual-specificity tyrosine phosphorylation-regulated kinase that phosphorylates a variety of substrates involved in cell cycle regulation, neurogenesis, and neuronal function. It is a serine/threonine protein kinase that is thought to play a role in the development and function of the central nervous system.

More about "DYRK1A protein, human"

DYRK1A, also known as Dual-Specificity Tyrosine Phosphorylation-Regulated Kinase 1A, is a crucial protein kinase that plays a pivotal role in various cellular processes.
This enzyme is expressed in both the nucleus and cytoplasm, and its dysregulation has been implicated in several neurological disorders, including Alzheimer's disease and Down syndrome.
DYRK1A is responsible for regulating the cell cycle, neuronal development, and signal transduction pathways.
It belongs to the DYRK family of kinases, which are involved in diverse cellular functions.
The DYRK1A protein can phosphorylate both tyrosine and serine/threonine residues, making it a dual-specificity kinase.
Researchers studying DYRK1A often utilize a variety of tools and techniques, such as the IRDye 800CW goat anti-mouse IgG antibody for detection, the TRIzol reagent for RNA extraction, and the Anti-FLAG M2 affinity gel for protein purification.
The FlexStation 3 multi-mode microplate reader and the Maestro imaging system are also commonly used to analyze DYRK1A-related experiments.
To ensure the accuracy and reproducibility of their research, scientists may turn to the PubCompare.ai platform, which employs artificial intelligence to help identify the most effective products and protocols for DYRK1A studies.
This innovative tool can enhance the quality and consistency of DYRK1A research, ultimately contributing to a better understanding of this important protein and its role in various disease processes.
Whether you are investigating the cellular functions of DYRK1A, exploring its involvement in neurological disorders, or developing therapeutic interventions targeting this kinase, PubCompare.ai can be a valuable resource to support your research endeavors.