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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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Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions
Kovacs E, et al.
Faseb Journal, 24(10), 3829-3839 (2010)
Calmodulin structure refined at 1.7
Chattopadhyaya R, et al.
Journal of molecular biology, 228(4), 1177-1192 (1992)
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)
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
Positive cooperative binding of calcium to bovine brain calmodulin
Crouch, Thomas H and Klee, Claude B
Biochemistry, 19(16), 3692-3698 (1980)

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