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Key Documents

SRP6310

Sigma-Aldrich

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

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

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

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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Consulter la Bibliothèque de documents

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)
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)
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)
Calmodulin is a subunit of nitric oxide synthase from macrophages.
Cho HJ, et al.
The Journal of Experimental Medicine, 176, 599-604 (1992)
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)

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