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Merck
모든 사진(1)

Key Documents

C4874

Sigma-Aldrich

Calmodulin bovine

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

동의어(들):

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

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About This Item

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

생물학적 소스

bovine

Quality Level

재조합

expressed in E. coli

분석

≥98% (SDS-PAGE)

형태

lyophilized powder

분자량

Mw 19000.9 by amino acid sequence

구성

Protein, ≥85%

UniProt 수납 번호

저장 온도

−20°C

유전자 정보

bovine ... CALM(100297344)

일반 설명

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.

애플리케이션

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.

생화학적/생리학적 작용

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.

물리적 특성

Sequence:
MGSSHHHHHHSSGLVPRGSHMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK

제조 메모

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


시험 성적서(COA)

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문서 라이브러리 방문

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)
Calmodulin structure refined at 1.7
Chattopadhyaya R, et al.
Journal of molecular biology, 228(4), 1177-1192 (1992)
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)
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)

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