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SRP0245

Sigma-Aldrich

DYRK2 Active human

recombinant, expressed in baculovirus infected insect cells, ≥50% (SDS-PAGE)

Synonym(s):

dual specificity tyrosine-phosphorylation-regulated kinase 2

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected insect cells

Assay

≥50% (SDS-PAGE)

form

aqueous solution

mol wt

63.5 kDa

packaging

pkg of 10 μg

concentration

>0.02 mg/mL

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... DYRK2(8445)

General description

Human DYRK2 (GenBank Accession No. NM_003583), full length with N-terminal His tag, MW = 63.5 kDa, expressed in Baculovirus infected Sf9 cell expression system.

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Physical form

TBST+20% glycerol+3mM DTT

Preparation Note

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

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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Rosario Morrugares et al.
Cellular and molecular life sciences : CMLS, 77(13), 2621-2639 (2019-10-13)
NOTCH proteins constitute a receptor family with a widely conserved role in cell cycle, growing and development regulation. NOTCH1, the best characterised member of this family, regulates the expression of key genes in cell growth and angiogenesis, playing an essential
Isao Kii et al.
Nature communications, 7, 11391-11391 (2016-04-23)
Autophosphorylation of amino-acid residues is part of the folding process of various protein kinases. Conventional chemical screening of mature kinases has missed inhibitors that selectively interfere with the folding process. Here we report a cell-based assay that evaluates inhibition of
Martin Mehnert et al.
Nature communications, 11(1), 3563-3563 (2020-07-18)
Rapidly increasing availability of genomic data and ensuing identification of disease associated mutations allows for an unbiased insight into genetic drivers of disease development. However, determination of molecular mechanisms by which individual genomic changes affect biochemical processes remains a major

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