D7194
DAPK3, active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Sinônimo(s):
FLJ36473, ZIP
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About This Item
Código UNSPSC:
12352200
NACRES:
NA.32
recombinante
expressed in baculovirus infected Sf9 cells
Nível de qualidade
linha de produto
PRECISIO® Kinase
Ensaio
≥70% (SDS-PAGE)
Formulário
buffered aqueous glycerol solution
atividade específica
32-43 nmol/min·mg
peso molecular
~79 kDa
nº de adesão UniProt
Condições de expedição
dry ice
temperatura de armazenamento
−70°C
Informações sobre genes
human ... DAPK3(1613)
Ações bioquímicas/fisiológicas
DAPK3 or Death-associated protein kinase 3 (also known as ZIP) plays a role in apoptosis.DAPK3 is a nuclear serine/threonine-specific kinase that phosphorylates core histones H3 and H4, and myosine light chain in vitro. DAPK3 interacts with transcription and splicing factors as well as with pro-apoptotic protein Par-4 suggesting that it participates in multiple cellular processes. DAPK3 contains a leucine zipper structure at its C terminus and this region is responsible for binding to ATF4. The leucine zipper domain is necessary for the homodimerization of DAPK3 as well as for the activation of the kinase.
forma física
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
Informações legais
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Ute Preuss et al.
Nucleic acids research, 31(3), 878-885 (2003-02-01)
Death-associated protein (DAP)-like kinase (Dlk), also known as Zipper interacting protein (ZIP) kinase, is a nuclear serine/threonine-specific kinase that phosphorylates core histones H3 and H4, and myosine light chain in vitro. It interacts with transcription and splicing factors as well
T Kawai et al.
Molecular and cellular biology, 18(3), 1642-1651 (1998-03-06)
We have identified a novel serine/threonine kinase, designated ZIP kinase, which mediates apoptosis. ZIP kinase contains a leucine zipper structure at its C terminus, in addition to a kinase domain at its N terminus. ZIP kinase physically binds to ATF4
Kasturi Markandran et al.
International journal of molecular sciences, 23(1) (2022-01-12)
Heart failure (HF) as a result of myocardial infarction (MI) is a major cause of fatality worldwide. However, the cause of cardiac dysfunction succeeding MI has not been elucidated at a sarcomeric level. Thus, studying the alterations within the sarcomere
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