C0874
CAMK2δ, active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
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MGC44911
Recommended Products
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
4981-6739 nmol/min·mg
mol wt
~77 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CAMK2D(817)
Biochem/physiol Actions
CAMK2δ is a serine/threonine protein kinase that is a member of the type II multifunctional Ca2+/calmodulin-dependent protein kinase family. CAMK2δ is abundantly present in human cardiac and skeletal muscle and its levels are increased in the heart of patients suffering from cardiomyopathy. In cardiomyocytes, stimulation of beta-1-adrenergic receptor leads to induction of apoptosis, an effect that is mediated by activation of CAMK2δ in a PKA-independent manner. In addition, expression studies have revealed the downregulation of CAMK2δ in human tumor cells.
Physical form
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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The Journal of clinical investigation, 111(5), 617-625 (2003-03-06)
beta(1)-adrenergic receptor (beta(1)AR) stimulation activates the classic cAMP/protein kinase A (PKA) pathway to regulate vital cellular processes from the change of gene expression to the control of metabolism, muscle contraction, and cell apoptosis. Here we show that sustained beta(1)AR stimulation
Circulation research, 84(6), 713-721 (1999-04-03)
Despite its importance for the regulation of heart function, little is known about the isoform expression of the multifunctional Ca2+/calmodulin-dependent protein kinase (CaMKII) in human myocardium. In this study, we investigated the spectrum of CaMKII isoforms delta2, delta3, delta4, delta8
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