SCP0001
Autocamptide-2 Related Inhibitor Peptide
Synonyme(s) :
AIP
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About This Item
Formule empirique (notation de Hill):
C78H142N22O20
Poids moléculaire :
1708.10
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
Pureté
≥95% (HPLC)
Forme
lyophilized
Composition
Peptide Content, ≥70%
Conditions de stockage
protect from light
Température de stockage
−20°C
Amino Acid Sequence
Myr-Lys-Lys-Ala-Leu-Arg-Arg-Gln-Glu-Ala-Val-Asp-Ala-Leu
Application
Autocamptide-2 Related Inhibitor Peptide (AIP) is highly specific inhibitor of calmodulin-dependent protein kinase II (CaMKII) that may be used to study the role of CaMKII in processes such as heart failure.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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CaMKII inhibition in heart failure makes jump to human.
Donald M Bers
Circulation research, 107(9), 1044-1046 (2010-10-30)
Wei Zhang et al.
Journal of cardiovascular pharmacology, 55(1), 96-105 (2009-11-26)
Calcium-calmodulin-dependent protein kinase II (CaMKII) is one of the main protein kinases mediating intracellular Ca changes. It is also involved in the process of cardiac diseases, such as cardiac hypertrophy, but its effects on myocardial fibrosis remain unclear. The present
Vassilios J Bezzerides et al.
Circulation, 140(5), 405-419 (2019-06-04)
Catecholaminergic polymorphic ventricular tachycardia (CPVT), an inherited cardiac arrhythmia characterized by adrenergically triggered arrhythmias, is inadequately treated by current standard of care. Ca2+/calmodulin-dependent protein kinase II (CaMKII), an adrenergically activated kinase that contributes to arrhythmogenesis in heart disease models, is
Keiichi Odagiri et al.
Journal of molecular and cellular cardiology, 46(6), 989-997 (2009-03-26)
Calmodulin (CaM) and Ca(2+)/CaM-dependent protein kinase II (CaMKII) play important roles in the development of heart failure. In this study, we evaluated the effects of CaM on mitochondrial membrane potential (DeltaPsi(m)), permeability transition pore (mPTP) and the production of reactive
A Ishida et al.
FEBS letters, 427(1), 115-118 (1998-06-05)
The importance of the individual amino acid residues of AIP (KKALRRQEAVDAL), a highly specific inhibitor of calmodulin-dependent protein kinase II (CaMKII), was studied. Replacement of Arg6, Gln7, or Ala9 by other amino acid residues produced a marked increase in the
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