Skip to Content
Merck
All Photos(1)

Key Documents

208921

Sigma-Aldrich

Calmodulin Kinase IINtide, Myristoylated

≥95% (HPLC), solid, CaMK II inhibitor, Calbiochem®

Synonym(s):

Calmodulin Kinase IINtide, Myristoylated, Myr-N-GGGKRPPKLGQIGRAKRVVIEDDRIDDVLK-OH

Sign Into View Organizational & Contract Pricing


About This Item

Empirical Formula (Hill Notation):
C256H275N47O43
Molecular Weight:
4698.21
UNSPSC Code:
12352200
NACRES:
NA.54

product name

Calmodulin Kinase IINtide, Myristoylated, The myristoylated form of CaMK IINtide.

Quality Level

Assay

≥95% (HPLC)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)

color

white

solubility

DMSO: 5 mg/mL

shipped in

ambient

storage temp.

−20°C

General description

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.

Biochem/physiol Actions

Cell permeable: yes
Primary Target
Calmodulin-Dependent Protein Kinase (CaM Kinase)-2
Product does not compete with ATP.
Reversible: no
Target IC50: 50 nM against cam Kinase-2

Packaging

Packaged under inert gas

Warning

Toxicity: Standard Handling (A)

Sequence

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

Physical form

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.

Other Notes

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.

Legal Information

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Synaptic memory survives molecular turnover.
Lee, et al.
Proceedings of the National Academy of Sciences of the USA, 119, e2211572119-e2211572119 (2023)
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
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)
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service