SRP6310
Calmodulin from bovine brain
≥95% (SDS-PAGE)
Synonyme(s) :
CALM, CAM
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About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
bovine brain
Pureté
≥95% (SDS-PAGE)
Forme
lyophilized
Poids mol.
16 kDa
Conditionnement
pkg of 1 mg
pkg of 500 μg
Adéquation
suitable for chromatography
Numéro d'accès UniProt
Conditions d'expédition
wet ice
Température de stockage
−20°C
Informations sur le gène
bovine ... CAM(520277)
Description générale
Calmodulin (CaM) is a ubiquitous, calcium-binding protein. CaM is expressed in many cell types and can have different subcellular locations, including the cytoplasm, within organelles, or associated with the plasma or organelle membranes. Many of the proteins that CaM binds are unable to bind calcium themselves, and as such use CaM as a calcium sensor and signal transducer. CaM can also make use of the calcium stores in the endoplasmic reticulum, and the sarcoplasmic reticulum. CaM undergoes a conformational change upon binding to calcium, which enables it to bind to specific proteins for a specific response.
Application
Calmodulin from bovine brain has been used to study calmodulin-associated endothelium-derived relaxing factor/nitric oxide synthase activity in the particulate and cytosolic fractions of bovine aortic endothelial cells. It has also been used as a standard in size-exclusion chromatography.
Actions biochimiques/physiologiques
Calmodulin (CaM) can bind to and regulate a multitude of different protein targets, thereby affecting many different cellular functions. It is involved in inflammation, metabolism, apoptosis, muscle contraction, intracellular movement, short-term and long-term memory, nerve growth and the immune response. CaM can bind up to four calcium ions, and can undergo post-translational modifications, such as phosphorylation, acetylation, methylation and proteolytic cleavage, each of which can potentially modulate its actions.
Forme physique
Lyophilized in 30 mM Hepes, pH 7.4, 1 mM CaCl2 and 0.1 mM DTT.
Reconstitution
In water or aqueous buffer
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin.
Magnani R, et al.
Nature Communications, 43, doi: 10-doi: 10 (2010)
Ca2+ binding and conformational change in two series of point mutations to the individual Ca(2+)-binding sites of calmodulin.
Maune JF, et al.
The Journal of Biological Chemistry, 267, 5286-5295 (1992)
Calmodulin-dependent endothelium-derived relaxing factor/nitric oxide synthase activity is present in the particulate and cytosolic fractions of bovine aortic endothelial cells.
Forstermann U, et al.
Proceedings of the National Academy of Sciences of the USA, 88, 1788-1792 (1991)
Calmodulin is a subunit of nitric oxide synthase from macrophages.
Cho HJ, et al.
The Journal of Experimental Medicine, 176, 599-604 (1992)
Intestinal calmodulin and calcium-binding protein differ in their distribution and in the effect of vitamin D steroids on their concentration.
Thomasset M, et al.
Febs Letters, 127, 13-16 (1981)
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