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C4874

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

UNSPSC Code:
12352202
NACRES:
NA.26
MDL number:
Form:
lyophilized powder
Assay:
≥98% (SDS-PAGE)
Biological source:
bovine
Recombinant:
expressed in E. coli
Mol wt:
Mw 19000.9 by amino acid sequence
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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

Sequence:
MGSSHHHHHHSSGLVPRGSHMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
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.

Preparation Note

Produced using animal component-free materials.

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This Item
P1431SRP6310P0270
assay

≥98% (SDS-PAGE)

assay

≥98% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

-

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

biological source

bovine

biological source

bovine testis

biological source

bovine brain

biological source

bovine heart

form

lyophilized powder

form

lyophilized powder

form

lyophilized

form

lyophilized powder

mol wt

Mw 19000.9 by amino acid sequence

mol wt

16.79 kDa

mol wt

16 kDa

mol wt

-

UniProt accession no.

P62157

UniProt accession no.

P62157

UniProt accession no.

P62157

UniProt accession no.

P62157


Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_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)



Global Trade Item Number

SKUGTIN
C4874-0.5MG04061833218013
C4874-2MG04061833493182
C4874-0.2MG04061833218006
C4874-1MG04061826703069

Questions

  1. How was the protein lyophilized? What was the buffer, it's concentration and volume?

    1 answer
    1. This product is dialyzed in water before lyophilization and contains no buffers, salts or additives. The material is soluble in water at 1 mg/mL. For assay purposes, the product is reconstituted at 1 mg/mL in 0.85% NaCl.

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