SRP6310
Calmodulin from bovine brain
≥95% (SDS-PAGE)
Sinonimo/i:
CALM, CAM
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About This Item
Codice UNSPSC:
12352200
NACRES:
NA.32
Prodotti consigliati
Origine biologica
bovine brain
Saggio
≥95% (SDS-PAGE)
Forma fisica
lyophilized
PM
16 kDa
Confezionamento
pkg of 1 mg
pkg of 500 μg
Compatibilità
suitable for chromatography
N° accesso UniProt
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
Informazioni sul gene
bovine ... CAM(520277)
Descrizione generale
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.
Applicazioni
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.
Azioni biochim/fisiol
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.
Stato fisico
Lyophilized in 30 mM Hepes, pH 7.4, 1 mM CaCl2 and 0.1 mM DTT.
Ricostituzione
In water or aqueous buffer
Avvertenze
Warning
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Eye Irrit. 2
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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 methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin.
Magnani R, et al.
Nature Communications, 43, doi: 10-doi: 10 (2010)
Teaching Molecular Biology using computational tools and tacking into account the learning styles of students.
Craciun D and Isvoran A
Romanian Biotechnological Letters, 14.4, 4567-4574 (2009)
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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