TECHNICAL SPECIFICATIONS
| Item | Specification |
|---|---|
| Product Name | Calmodulin-Dependent Protein Kinase II (281 – 289) |
| CAS NO. | / |
| Appearance | White to off-white lyophilized powder |
| Molecular Formula | C43H71N15O16S2 |
| Molecular Weight | 1118.26 g/mol |
| Purity (RP-HPLC) | ≥ 95.0% |
| Solubility | Soluble in water, PBS (pH 7-8), dilute acetic acid |
| Endotoxin | < 1.0 EU/mg |
| Biological Activity | The self-inhibition domain fragment of CaMKII can competitively bind to the catalytic domain of CaMKII, simulating a self-inhibition state, and can be used to study the activation/inhibition mechanism, enzyme activity regulation, and signal transduction of CaMKII. |
| Storage Conditions | Store at -20°C or below, protected from light and moisture. After reconstitution, aliquot and store at -20°C |
| Stock Location | Stock in USA |
| MOQ | 1g |
Calmodulin-Dependent Protein Kinase II (281-289) functions as a competitive inhibitor by binding to the catalytic domain of CaMKII, mimicking the autoinhibitory interaction that occurs in the inactive state of the full-length enzyme. In the absence of calcium/calmodulin, this peptide sequence in the intact CaMKII associates with the catalytic site, preventing substrate access and maintaining the kinase in an inactive conformation. The synthetic peptide competes with the endogenous autoinhibitory domain for binding to the catalytic site, thereby inhibiting CaMKII activity. This inhibition is reversible and concentration-dependent, allowing researchers to specifically probe CaMKII function without affecting other kinases. The peptide's mechanism is based on its high-affinity interaction with the catalytic domain, effectively blocking substrate phosphorylation and downstream signaling events.
Comparative Studies: Assessment of CaMKII isoform-specific regulation and function CaMKII Activity Studies: Competitive inhibition assays to measure kinase activity and IC₅₀ determination
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