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Key Documents

SRP6310

Sigma-Aldrich

Calmodulin from bovine brain

≥95% (SDS-PAGE)

Synonym(s):

CALM, CAM

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

bovine brain

Assay

≥95% (SDS-PAGE)

form

lyophilized

mol wt

16 kDa

packaging

pkg of 1 mg
pkg of 500 μg

suitability

suitable for chromatography

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

bovine ... CAM(520277)

General description

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.

Biochem/physiol Actions

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.

Physical form

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

Reconstitution

In water or aqueous buffer

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Eye Irrit. 2

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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

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