recombinant
expressed in baculovirus infected Sf9 cells
product line
PRECISIO® Kinase
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
63-72 nmol/min·mg
mol wt
~64 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CSNK2A2(1459)
General description
CK2α2 or casein kinase II alpha 2 is a member of the CK2 family of Ser/Thr protein kinases. CK2a2 plays a fundamental role in cell function and is involved in DNA replication, regulation of basal and inducible transcription, translation and control of metabolism. CK2α2 prefers utilization of acidic proteins such as caseins as substrates. The CK2a2 holoenzyme is a tetramer composed of an alpha chain, an alpha′ and two beta chains. The alpha and alpha′ chains contain the catalytic site. CK2α2 is also a component of CK2-SPT16-SSRP1 complex comprised of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. This complex associates following UV irradiation. CK2a2 act as a candidate gene for inherited abnormalities of sperm morphogenesis.
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
X Xu et al.
Nature genetics, 23(1), 118-121 (1999-09-02)
Protein kinase casein kinase II (Ck2) is a cyclic-AMP and calcium-independent serine-threonine kinase that is composed of two catalytic subunits (alpha and alpha') and two regulatory beta-subunits. Ck2 is not a casein kinase in vivo, but over 100 substrates are
D M Keller et al.
Molecular cell, 7(2), 283-292 (2001-03-10)
Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not gamma irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro.
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