Analytical Data
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Gene name
DYRK4
- Application
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Alternative Names
DYRK4Dual specificity tyrosine-phosphorylation-regulated kinase 4; EC 2.7.12.1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NR20
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Expression Region
1-520aa
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AA Sequence
MPASELKASEIPFHPSIKTQDPKAEEKSPKKQKVTLTAAEALKLFKNQLSPYEQSEILGYAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPRPQTLRKSNSFFPSETRKDKVQGCHHSSRKADEITKETTEKTKDSPTKHVQHSGDQQDCLQHGADTVQLPQLVDAPKKSEAAVGAEVSMTSPGQSKNFSLKNTNVLPPIV
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Molecular Weight
86 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
DYRK4 (Dual-specificity tyrosine-phosphorylation-regulated kinase 4) is a member of the DYRK family of protein kinases, which are known for their role in various cellular processes including cell differentiation, proliferation, and apoptosis. Recent studies have indicated that DYRK4 plays a crucial role in the regulation of neuronal development and function, suggesting its importance in neurodegenerative diseases and cognitive disorders. Given its dual-specificity, DYRK4 can phosphorylate both serine/threonine and tyrosine residues, making it a potential target for therapeutic intervention. The recombinant protein of DYRK4 is being increasingly studied in order to elucidate its structure-function relationships and to develop inhibitors that can modulate its activity. Current research involves the expression and purification of the DYRK4 recombinant protein to facilitate biochemical assays, structural studies, and potential drug discovery efforts. By understanding the molecular mechanisms underlying DYRK4's actions, researchers aim to uncover new insights into its role in health and disease, ultimately paving the way for novel therapeutic strategies targeting DYRK4-related pathways.
