重組細胞
expressed in baculovirus infected Sf9 cells
品質等級
產品線
PRECISIO® Kinase
化驗
≥70% (SDS-PAGE)
形狀
buffered aqueous glycerol solution
比活性
32-43 nmol/min·mg
分子量
~79 kDa
UniProt登錄號
運輸包裝
dry ice
儲存溫度
−70°C
基因資訊
human ... DAPK3(1613)
生化／生理作用
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.
外觀
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.
法律資訊
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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