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Merck
CN

SCP0212

Sigma-Aldrich

PKA Substrate

≥95% (HPLC), lyophilized

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About This Item

经验公式(希尔记法):
C39H74N20O12
分子量:
1015.13
UNSPSC代码:
12352204
NACRES:
NA.32

product name

PKA Substrate,

检测方案

≥95% (HPLC)

形式

lyophilized

组成

Peptide Content, ≥60%

储存条件

protect from light

储存温度

−20°C

Amino Acid Sequence

Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ser-Ile-NH2

一般描述

cAMP-dependent protein kinase (PKA) Substrate (GRTGRRNSI-NH2) is a nine amino acid phosphorylatable substrate of cyclic adenosine monophosphate (cAMP)-dependent protein kinase.

应用

cAMP-dependent protein kinase (PKA) Substrate has been used as a peptide substrate for Plasmodium cyclic guanosine monophosphate (GMP)-dependent protein kinase in enzymatic assay and inhibition assay. It has also been used as a positive control in the in vitro protein kinase A (PKA) phosphorylation assay.

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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Michael J Moore et al.
The Journal of biological chemistry, 278(12), 10613-10618 (2002-12-25)
For optimal activity the catalytic subunit of cAMP-dependent protein kinase requires a phosphate on Thr-197. This phosphate anchors the activation loop in the proper conformation and contributes to catalytic efficiency by enhancing the phosphoryl transfer rate and increasing the affinity
Jacqueline B Pierce et al.
Eukaryotic cell, 13(2), 209-230 (2013-12-04)
The two main signal transduction mechanisms that allow eukaryotes to sense and respond to changes in glucose availability in the environment are the cyclic AMP (cAMP)/protein kinase A (PKA) and AMP-activated protein kinase (AMPK)/Snf1 kinase-dependent pathways. Previous studies have shown
Q Ni et al.
Protein science : a publication of the Protein Society, 9(9), 1818-1827 (2000-10-25)
The binding of the methylanthraniloyl derivatives of ATP (mant-ATP), ADP (mant-ADP), 2'deoxyATP (mant-2'deoxyATP), and 3'deoxyATP (mant-3'deoxyATP) to the catalytic subunit of protein kinase A was studied to gain insights into the mechanism of nucleotide binding. The binding of the mant
Maria Penzo et al.
Scientific reports, 9(1), 7005-7005 (2019-05-09)
Antimalarial drug resistance compels the quest for new compounds that target alternative pathways to current drugs. The Plasmodium cyclic GMP-dependent protein kinase (PKG) has essential functions in all of the major life cycle developmental stages. An imidazopyridine PKG inhibitor scaffold
Manu Vanaerschot et al.
Cell chemical biology, 27(7), 806-816 (2020-05-04)
The search for antimalarial chemotypes with modes of action unrelated to existing drugs has intensified with the recent failure of first-line therapies across Southeast Asia. Here, we show that the trisubstituted imidazole MMV030084 potently inhibits hepatocyte invasion by Plasmodium sporozoites

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