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Key Documents

C4874

Sigma-Aldrich

Calmodulin bovine

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

Synonym(s):

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

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.26

biological source

bovine

Quality Level

recombinant

expressed in E. coli

Assay

≥98% (SDS-PAGE)

form

lyophilized powder

mol wt

Mw 19000.9 by amino acid sequence

composition

Protein, ≥85%

UniProt accession no.

storage temp.

−20°C

Gene Information

bovine ... CALM(100297344)

General description

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.

Application

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.

Biochem/physiol Actions

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.

Physical properties

Sequence:
MGSSHHHHHHSSGLVPRGSHMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK

Preparation Note

Produced using animal component-free materials.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5
Liu S, et al.
Amino Acids, 48(4), 1059-1067 (2016)
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
Junxia Zhang et al.
Circulation, 145(15), 1154-1168 (2022-03-24)
Cardiac ischemia/reperfusion (I/R) injury has emerged as an important therapeutic target for ischemic heart disease, the leading cause of morbidity and mortality worldwide. At present, there is no effective therapy for reducing cardiac I/R injury. CaMKII (Ca2+/calmodulin-dependent kinase II) plays
Phosphorylation-dependent feedback inhibition of RIG-I by DAPK1 identified by kinome-wide siRNA screening
Willemsen J, et al.
Molecular Cell, 65(3), 403-415 (2017)
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

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