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Merck
CN

370655

Sigma-Aldrich

PKG Iα Inhibitor, Cell-Permeable

The PKG Iα Inhibitor, Cell-Permeable controls the biological activity of PKG Iα. This small molecule/inhibitor is primarily used for Phosphorylation & Dephosphorylation applications.

别名:

PKG Iα Inhibitor, Cell-Permeable, DT-3, RQIKIWFQNRRMKWKKLRKKKKKH, PKG Inhibitor VIII

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关于此项目

经验公式（希尔记法）:
C152H258N52O28S
分子量:
3294.07
UNSPSC代码:
12352200
NACRES:
NA.77

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质量水平

100

方案

≥95% (HPLC)

表单

lyophilized

制造商/商品名称

Calbiochem®

储存条件

OK to freeze
desiccated (hygroscopic)

溶解性

DMSO: 10 mg/mL

运输

ambient

储存温度

−20°C

相关类别

一般描述

A highly potent, reversible, and substrate competitive membrane-permeable peptide that selectively inhibits protein kinase G Iα (PKG Iα) (Ki = 25 nM). Inhibitor peptide is fused to the Drosophila Antennapedia homeo domain peptide to allow membrane permeability. Shown to efficiently cross the membrane of arterial smooth muscle cells and inhibit nitric oxide-induced (NO-induced) vasodilation (EC50 = 47 µM). Inhibits protein kinase A (PKA) activity only at much higher concentrations (Ki = 493 µM). The carrier peptide is also available under Cat. no. 287895.

生化/生理作用

Cell permeable: yes
Primary Target
PKG1α
Product competes with ATP.
Reversible: yes
Target Ki: 25 nM against protein kinase G Iα

包装

Packaged under inert gas

外形

Supplied as a trifluoroacetate salt.

制备说明

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 2 months at -20°C.

其他说明

Dostmann, W. R.G., et al. 2000. Proc. Natl. Acad. Sci. USA 97, 14772.
H-Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys-Leu-Arg-Lys-Lys-Lys-Lys-Lys-His-OH

法律信息

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

免责声明

Toxicity: Standard Handling (A)

储存分类代码

11 - Combustible Solids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

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Malgorzata Szaroszyk et al.
Nature communications, 13(1), 149-149 (2022-01-12)
Cachexia is associated with poor prognosis in chronic heart failure patients, but the underlying mechanisms of cachexia triggered disease progression remain poorly understood. Here, we investigate whether the dysregulation of myokine expression from wasting skeletal muscle exaggerates heart failure. RNA

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