推荐产品
product name
Phospho-Glycogen Synthase Peptide-2, Phospho-Glycogen Synthase Peptide-2 primarily used in Kinase Assays.
质量水平
形式
lyophilized
制造商/商品名称
Upstate®
技术
activity assay: suitable (kinase)
运输
wet ice
质量
Routinely evaluated as a substrate of active GSK3β (Catalog # 14-306) to catalyze the incorporation of phosphate into phospho-glycogen synthase peptide-2.
储存及稳定性
Lyophilized: Stable for 2 years at -20°C from date of shipment. Rehydrated: Stable for 6 months at -20°C. Aliquot rehydrated solution to avoid repeated freezing and thawing.
法律信息
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Use of peptide substrates for affinity purification of protein-serine kinases.
Woodgett, J R
Analytical biochemistry, 180, 237-241 (1989)
C M Moxham et al.
The Journal of biological chemistry, 271(48), 30765-30773 (1996-11-29)
Mitogen-activated protein kinases (MAPKs) represent a conserved family of Ser/Thr protein kinases with central roles in intracellular signaling. Activation of three prominent members of the MAPK family, i.e. extracellular response kinases (ERK), jun N-terminal kinase (JNK), and p38, was defined
Regulation of glycogen synthase kinase-3 in human skeletal muscle: effects of food intake and bicycle exercise
Wojtaszewski, J. F., et al
Diabetes, 50, 265-269 (2001)
S R Kimball et al.
The Journal of biological chemistry, 273(47), 30945-30953 (1998-11-13)
The present study was designed to investigate the mechanism through which leucine and histidine regulate translation initiation in L6 myoblasts. The results show that both amino acids stimulate initiation and coordinately regulate the activity of eukaryotic initiation factor eIF2B. The
M Pap et al.
The Journal of biological chemistry, 273(32), 19929-19932 (1998-08-01)
Growth factor-dependent survival of a variety of mammalian cells is dependent on the activation of phosphatidylinositol (PI) 3-kinase and its downstream effector, the protein kinase Akt. Glycogen synthase kinase-3 (GSK-3) has been previously identified as a physiological target of Akt
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