P3115
Protein Kinase C Inhibitor, Myristoylated
≥7.5 mg/mL (peptide and counter ion), ≥95% (Minimum peptide content 70%, HPLC), aqueous solution (neutral pH)
别名:
Myr-Arg-Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val, Myr-RFARKGALRQKNV
生物来源
synthetic (organic
organic)
方案
≥95% (Minimum peptide content 70%, HPLC)
表单
aqueous solution (neutral pH)
分子量
1,754.3 Da (Fast Atomic Bombardment Mass Spectrometry)
1.75 kDa
组成
Peptide content, ≥70%
浓度
≥7.5 mg/mL (peptide and counter ion)
运输
dry ice
储存温度
−20°C
应用
Protein Kinase C (PKC) Inhibitor, Myristoylated is supplied ready for use in kinase reactions. An inhibitor peptide (concentration of 50 to 100 μM) is recommended, depending on the concentration of PKC and the duration of the incubation.
生化/生理作用
Protein Kinase C Inhibitor, Myristoylated is a cell permeable, specific inhibitor of calcium and phospholipid-dependent Protein Kinase C.
储存分类代码
10 - Combustible liquids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
T Eichholtz et al.
The Journal of biological chemistry, 268(3), 1982-1986 (1993-01-25)
Synthetic peptides corresponding to the pseudosubstrate domains of protein kinase C (PKC) have been used as specific inhibitors of PKC in in vitro assays and permeabilized cell systems. However, their use in vivo was hampered by the impermeability of the
Katarzyna Bialkowska et al.
The Journal of biological chemistry, 290(10), 6226-6242 (2015-01-23)
The contributions of integrins to cellular responses depend upon their activation, which is regulated by binding of proteins to their cytoplasmic tails. Kindlins are integrin cytoplasmic tail binding partners and are essential for optimal integrin activation, and kindlin-3 fulfills this
Hongwei Si et al.
Endocrinology, 153(7), 3190-3198 (2012-06-07)
We previously reported that genistein, a phytoestrogen, up-regulates endothelial nitric oxide synthase (eNOS) and prevents hypertension in rats that are independent of estrogen signaling machinery. However, how genistein regulates eNOS expression is unknown. In the present study, we show that
Samantha L Yuen et al.
American journal of physiology. Heart and circulatory physiology, 297(1), H191-H199 (2009-05-12)
The participation of nonmuscle myosin in force maintenance is controversial. Furthermore, its regulation is difficult to examine in a cellular context, as the light chains of smooth muscle and nonmuscle myosin comigrate under native and denaturing electrophoresis techniques. Therefore, the
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