Analytical Data
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Gene name
DYRK2
- Application
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Alternative Names
/
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Species
Human
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Source
Baculovirus
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92630-2
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Expression Region
1-528aa
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Molecular Weight
61.7 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
DYRK2 (Dual-specificity tyrosine phosphorylation-regulated kinase 2) is a member of the DYRK family of kinases, which play significant roles in various cellular processes, including cell proliferation, differentiation, and apoptosis. The interest in DYRK2 has surged due to its involvement in several critical biological pathways and its potential implications in cancer and neurodegenerative diseases. Research has shown that DYRK2 can modulate the phosphorylation states of several key substrates, influencing cellular signaling networks. Additionally, DYRK2 is recognized for its regulatory functions in the cell cycle and its role in the response to cellular stress. The burgeoning understanding of DYRK2's mechanisms has paved the way for investigating its potential as a therapeutic target. Notably, the development of recombinant DYRK2 protein presents an opportunity to explore its biochemical properties, interactions, and kinase activity in greater detail. Such studies are essential for elucidating the role of DYRK2 in pathological conditions and can lead to the identification of novel drug candidates that specifically inhibit or activate this kinase. The growing body of evidence surrounding DYRK2 underscores the significance of understanding its functional dynamics through advanced molecular techniques, fostering advancements in targeted therapies and personalized medicine.
