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Documentos clave

C4874

Sigma-Aldrich

Calmodulin bovine

recombinant, expressed in E. coli, lyophilized powder, ≥98% (SDS-PAGE)

Sinónimos:

CaM, Phosphodiesterase 3:5-cyclic nucleotide activator, Phosphodiesterase 3′:5′-cyclic nucleotide activator

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About This Item

Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.26

origen biológico

bovine

Nivel de calidad

recombinante

expressed in E. coli

Ensayo

≥98% (SDS-PAGE)

Formulario

lyophilized powder

mol peso

Mw 19000.9 by amino acid sequence

composición

Protein, ≥85%

Nº de acceso UniProt

temp. de almacenamiento

−20°C

Información sobre el gen

bovine ... CALM(100297344)

Descripción general

Calmodulin from bovine takes up a dumb-bell-structure. Two calcium binding EF hand loops, antiparallel β-sheet and three α-helices comprises a lobe. It has a central helix connecting the lobes. Calmodulin can bind four calcium molecules in a cooperative interaction pattern.

Aplicación

Calmodulin bovine has been used inin vitro phosphorylation assay of recombinant retinoic acid-inducible gene I protein. It has also been used in the endoprotease Glu-C proteolysis and deamidation studies.

Acciones bioquímicas o fisiológicas

Ca2+ binding protein that is required for activation of cyclic nucleotide-dependent phosphodiesterase. It is also a cofactor/activator of nitric oxide synthase, calcineurin, and many kinases including ATPase, myosin light chain kinase, and CAM kinase I, II, and III. It mediates ryanodine receptor activation by cyclic ADP-ribose and is involved in intracellular Ca2+ homeostasis.
Calmodulin from bovine undergoes conformational changes upon calcium binding. It binds to sphingosylphosphorylcholine and inhibit calcineurin and phosphodiesterase enzymes.

Propiedades físicas

Sequence:
MGSSHHHHHHSSGLVPRGSHMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK

Nota de preparación

Produced using animal component-free materials.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Miljan Simonovic et al.
The Journal of biological chemistry, 281(45), 34333-34340 (2006-09-02)
AlphaII-spectrin is a major cortical cytoskeletal protein contributing to membrane organization and integrity. The Ca2+-activated binding of calmodulin to an unstructured insert in the 11th repeat unit of alphaII-spectrin enhances the susceptibility of spectrin to calpain cleavage but abolishes its
Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme.
Feng C., et al
Biochimica et Biophysica Acta (2011)
Does calmodulin regulate the bicarbonate permeability of ANO1/TMEM16A or not?
Jinsei Jung et al.
The Journal of general physiology, 145(1), 75-77 (2014-12-31)
Steve L Reichow et al.
Nature structural & molecular biology, 20(9), 1085-1092 (2013-07-31)
Calmodulin (CaM) is a universal regulatory protein that communicates the presence of calcium to its molecular targets and correspondingly modulates their function. This key signaling protein is important for controlling the activity of hundreds of membrane channels and transporters. However
Erika Kovacs et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 24(10), 3829-3839 (2010-06-05)
Lipid-protein interactions are rarely characterized at a structural molecular level due to technical difficulties; however, the biological significance of understanding the mechanism of these interactions is outstanding. In this report, we provide mechanistic insight into the inhibitory complex formation of

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