14-692-M
DAPK1 Protein, active, 10 µg
Active, N-terminal GST-tagged, recombinant, human DAPK1, amino acids 1-296, for use in Kinase Assays.
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About This Item
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biological source
human
Quality Level
100
300
recombinant
expressed in baculovirus infected Sf21 cells
mol wt
Mw 60.9 kDa
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
NCBI accession no.
UniProt accession no.
Gene Information
human ... DAPK1(1612)
General description
N-terminal GST-tagged, recombinant, human DAPK1, amino acids 1-296
Biochem/physiol Actions
Protein Target: DAPK1
Quality
routinely evaluated by phosphorylation of ZIPtide (Catalog #12-545)
Storage and Stability
stable 6 months at -70°C from date of shipment
Other Notes
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Skin Sens. 1
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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Find documentation for the products that you have recently purchased in the Document Library.
DAP-kinase as a target for drug design in cancer and diseases associated with accelerated cell death.
Seminars in cancer biology, 14, 283-294 (2004)
Epigenetic change in pituitary tumorigenesis.
Endocrine-Related Cancer, 10, 323-330 (2003)
Pharmacology & therapeutics, 93(2-3), 217-224 (2002-08-23)
Death-associated protein kinase (DAPK) is a calmodulin-regulated serine/threonine protein kinase associated with neuronal cell death in animal models of disease. The recent determination of the 1.5A crystal structure of the catalytic kinase domain of DAPK, the discovery of amino acid
The DAP-kinase family of proteins: study of a novel group of calcium-regulated death-promoting kinases.
Biochimica et Biophysica Acta, 1600, 45-50 (2002)
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