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
biological source
synthetic (organic
organic)
assay
≥95% (Minimum peptide content 70%, HPLC)
form
aqueous solution (neutral pH)
mol wt
1,754.3 Da (Fast Atomic Bombardment Mass Spectrometry), 1.75 kDa
composition
Peptide content, ≥70%
concentration
≥7.5 mg/mL (peptide and counter ion)
shipped in
dry ice
storage temp.
−20°C
Application
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.
Biochem/physiol Actions
Protein Kinase C Inhibitor, Myristoylated is a cell permeable, specific inhibitor of calcium and phospholipid-dependent Protein Kinase C.
存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
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
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
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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