Bioactive Proteins
Calmodulin
Please contact us to inquire about pricing for 100 mg and 1 g
Features
- Derived from bovine testes
- Calcium-binding protein
- Intracellular receptor protein
Product description
Calmodulin is a bioactive protein isolated from bovine testes. The material is derived fromindividually marked animals born and raised in Sweden, a country where BSE has not beena problem. Calmodulin is a calcium-binding protein expressed in many eukaryotic cells.By binding to and regulating various protein targets, it affects cellular processes such asmetabolism, nerve growth, apoptosis, inflammation, muscle contra ction and memory.
Calmodulin is used by many proteins as a calcium sensor and signal transducer, as theproteins themselves are not able to bind calcium. The molecule can bind a maximum offour calcium ions and by undergoing post-translational modificat ions such as acetylation,phosphorylation, proteolytic cleavage and methylation, its functions can potentially be altered.
Calmodulin is supplied as a lyophilized white powder or floccula te from 50 mM NH4HCO3 with10 μM CaCl2. No preservatives are added.
For laboratory use only.
Applications
- Protein calcium-binding studies on the regulation of a multitud e of different protein targets
- Activation of cyclic nucleotide-dependent phosphodiesterase
- Co-factor/activator for kinase studies
- Studies of edema factor toxin and anthrax bacteria
Directions for use
Dissolve the protein in desired buffer depending on your application.
Shipping and storage
Stable for at least 5 years from production date when stored at -20°C. May be shipped atambient temperature. After recon-stitution in PBS pH 7.4, the solution may be stored frozen inworking aliquots for up to 12 months. Repeated freezing and thawing is not recommended. Ifslight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.
Crystal structure of bovine Ca2+ calmodulin (1)
References
(1) A closed compact structure of native ca(2+)-calmodulin. Fallon, J.L., Quiocho, F.A.(2003) Structure 11: 1303 –7