SCP0001
Autocamptide-2 Related Inhibitor Peptide
Synonym(s):
AIP
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About This Item
Empirical Formula (Hill Notation):
C78H142N22O20
Molecular Weight:
1708.10
NACRES:
NA.32
UNSPSC Code:
12352202
assay
≥95% (HPLC)
form
lyophilized
composition
Peptide Content, ≥70%
storage condition
protect from light
storage temp.
−20°C
Related Categories
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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)
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
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
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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