208921
Calmodulin Kinase IINtide, Myristoylated
≥95% (HPLC), solid, CaMK II inhibitor, Calbiochem®
Synonyme(s) :
Calmodulin Kinase IINtide, Myristoylated, Myr-N-GGGKRPPKLGQIGRAKRVVIEDDRIDDVLK-OH
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About This Item
Formule empirique (notation de Hill):
C256H275N47O43
Poids moléculaire :
4698.21
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.54
Produits recommandés
product name
Calmodulin Kinase IINtide, Myristoylated, The myristoylated form of CaMK IINtide.
Niveau de qualité
Pureté
≥95% (HPLC)
Forme
solid
Fabricant/nom de marque
Calbiochem®
Conditions de stockage
OK to freeze
desiccated (hygroscopic)
Couleur
white
Solubilité
DMSO: 5 mg/mL
Conditions d'expédition
ambient
Température de stockage
−20°C
Description générale
The myristoylated form of CaMK IINtide (Cat. No. 208920). The peptide has been modified at the amino terminal lysine with the addition of three glycine residues and myristoylated to improve cell-permeability.
The myristoylated form of CaMK IINtide (Cat. No. 208920), a potent, specific inhibitor of Ca2+/Calmodulin kinase II (CaMK II) (IC50 = 50 nM for total and Ca2+-independent CaMK II activity). The peptide sequence corresponds to the inhibitory domain of the CaMK II inhibitory protein, CaMK IIN. Exhibits inhibitory activity across converged species, including rat brain, goldfish brain, and Drosophila (IC50 = 100-400 nM). Shown to completely inhibit the phosphorylation of GluR1 fusion protein at a concentration of 1 µM. Does not inhibit CaMK I, CaMK IV, CaMKK, PKA, or PKC. The peptide has been modified at the amino terminal lysine with the addition of three glycine residues and myristoylated to improve cell-permeability.
Actions biochimiques/physiologiques
Cell permeable: yes
Primary Target
Calmodulin-Dependent Protein Kinase (CaM Kinase)-2
Calmodulin-Dependent Protein Kinase (CaM Kinase)-2
Product does not compete with ATP.
Reversible: no
Target IC50: 50 nM against cam Kinase-2
Conditionnement
Packaged under inert gas
Avertissement
Toxicity: Standard Handling (A)
Séquence
Myr-N-Gly-Gly-Gly-Lys-Arg-Pro-Pro-Lys-Leu-Gly-Gln-Ile-Gly-Arg-Ala-Lys-Arg-Val-Val-Ile-Glu-Asp-Asp-Arg-Ile-Asp-Asp-Val-Leu-Lys-OH
Forme physique
Supplied as a trifluoroacetate salt.
Reconstitution
Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at-20°C.
Autres remarques
Sodering, T.R., et al. 2001. J. Biol. Chem.276, 3719.
Chang, B.H., et al. 1998. Proc. Natl. Acad. Sci. USA95, 10890.
Pereda, A.E., et al. 1998. Proc. Natl. Acad. Sci. USA95, 13272.
Chang, B.H., et al. 1998. Proc. Natl. Acad. Sci. USA95, 10890.
Pereda, A.E., et al. 1998. Proc. Natl. Acad. Sci. USA95, 13272.
Informations légales
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Synaptic memory survives molecular turnover.
Lee, et al.
Proceedings of the National Academy of Sciences of the USA, 119, e2211572119-e2211572119 (2023)
Xiumin Chen et al.
Proceedings of the National Academy of Sciences of the United States of America, 121(26), e2402783121-e2402783121 (2024-06-18)
Ca2+/calmodulin (CaM)-dependent kinase II (CaMKII) plays a critical role in long-term potentiation (LTP), a well-established model for learning and memory through the enhancement of synaptic transmission. Biochemical studies indicate that CaMKII catalyzes a phosphotransferase (kinase) reaction of both itself (autophosphorylation)
Wucheng Tao et al.
eLife, 10 (2021-12-16)
Long-term potentiation (LTP) is arguably the most compelling cellular model for learning and memory. While the mechanisms underlying the induction of LTP ('learning') are well understood, the maintenance of LTP ('memory') has remained contentious over the last 20 years. Here
Rabia Anjum et al.
PloS one, 19(7), e0301063-e0301063 (2024-07-12)
Synaptic plasticity, the process whereby neuronal connections are either strengthened or weakened in response to stereotyped forms of stimulation, is widely believed to represent the molecular mechanism that underlies learning and memory. The holoenzyme calcium/calmodulin-dependent protein kinase II (CaMKII) plays
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