SRP5170
CaMKPase, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
别名:
FEM-2, KIAA0015, POPX2, PPM1F, hFEM-2
重组
expressed in E. coli
方案
≥70% (SDS-PAGE)
表单
buffered aqueous glycerol solution
分子量
~74 kDa
NCBI登记号
运输
dry ice
储存温度
−70°C
基因信息
human ... PPM1F(9647)
一般描述
CaMKPase is a member of the PP2C family of Ser/Thr protein phosphatases that dephosphorylate and regulate the multifunctional Ca2+/calmodulin-dependent protein kinases (CaMKs). The multifunctional CaMKs mediate cellular responses induced by increases in second messenger Ca2+ and have been implicated in the control of synaptic transmission, gene transcription, cell growth and contraction of cardiac and smooth muscles. Overexpression of CaMKPase has been shown to mediate caspase-dependent apoptosis. CaMKPase can also interact with the Rho guanine nucleotide exchange factors (PIX) thereby blocking the effects of p21-activated kinase 1 (PAK1).
外形
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
制备说明
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
储存分类代码
10 - Combustible liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
新产品
此项目有
Atsuhiko Ishida et al.
Archives of biochemistry and biophysics, 408(2), 229-238 (2002-12-05)
Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKPase) dephosphorylates and regulates multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs). One of the prominent features of CaMKPase is stimulation of phosphatase activity by polycations such as poly-L-lysine (poly(Lys)). Using various polycations, basicity and molecular weight of the
I Kameshita et al.
FEBS letters, 456(2), 249-252 (1999-08-24)
Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKPase) is a protein phosphatase which dephosphorylates autophosphorylated Ca2+/calmodulin-dependent protein kinase II (CaMKII) and deactivates the enzyme (Ishida, A., Kameshita, I. and Fujisawa, H. (1998) J. Biol. Chem. 273, 1904-1910). In this study, a phosphorylation-dephosphorylation relationship
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