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
Form:
lyophilized powder
Assay:
≥98% (SDS-PAGE)
Biological source:
bovine
Recombinant:
expressed in E. coli
Mol wt:
Mw 19000.9 by amino acid sequence
biological source
bovine
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
Quality Level
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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
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)
Chihiro Nakajima et al.
The Analyst, 136(1), 113-119 (2010-10-12)
A method for de novo sequencing of N(α)-blocked proteins by mass spectrometry (MS) is presented. The approach consists of enzymatic digestion of N(α)-blocked protein, recovery of N-terminal peptide by depletion of non-N-terminal peptides from the digest pool, and selective derivatization
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)
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