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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About This Item
Form:
lyophilized powder
Assay:
≥98% (SDS-PAGE)
Biological source:
bovine
Recombinant:
expressed in E. coli
Mol wt:
Mw 19000.9 by amino acid sequence
Pricing and availability is not currently available.
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
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 | |||
|---|---|---|---|
| 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. | UniProt accession no. | UniProt accession no. | UniProt accession no. |
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
| SKU | GTIN |
|---|---|
| C4874-0.5MG | 04061833218013 |
| C4874-2MG | 04061833493182 |
| C4874-0.2MG | 04061833218006 |
| C4874-1MG | 04061826703069 |
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How was the protein lyophilized? What was the buffer, it's concentration and volume?
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