Direkt zum Inhalt
Merck

SRP6310

Sigma-Aldrich

Calmodulin from bovine brain

≥95% (SDS-PAGE)

Synonym(e):

CALM, CAM

Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise


About This Item

UNSPSC-Code:
12352200
NACRES:
NA.32

Biologische Quelle

bovine brain

Assay

≥95% (SDS-PAGE)

Form

lyophilized

Mol-Gew.

16 kDa

Verpackung

pkg of 1 mg
pkg of 500 μg

Eignung

suitable for chromatography

UniProt-Hinterlegungsnummer

Versandbedingung

wet ice

Lagertemp.

−20°C

Angaben zum Gen

bovine ... CAM(520277)

Allgemeine Beschreibung

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.

Anwendung

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.

Biochem./physiol. Wirkung

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.

Physikalische Form

Lyophilized in 30 mM Hepes, pH 7.4, 1 mM CaCl2 and 0.1 mM DTT.

Rekonstituierung

In water or aqueous buffer

Piktogramme

Exclamation mark

Signalwort

Warning

H-Sätze

Gefahreneinstufungen

Eye Irrit. 2

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

Besitzen Sie dieses Produkt bereits?

In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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)

Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..

Setzen Sie sich mit dem technischen Dienst in Verbindung.