추천 제품
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
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)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
Phosphorylation-dependent feedback inhibition of RIG-I by DAPK1 identified by kinome-wide siRNA screening
Molecular Cell, 65(3), 403-415 (2017)
Calmodulin structure refined at 1.7
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
Faseb Journal, 24(10), 3829-3839 (2010)
Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme.
Biochimica et Biophysica Acta (2011)
Does calmodulin regulate the bicarbonate permeability of ANO1/TMEM16A or not?
The Journal of general physiology, 145(1), 75-77 (2014-12-31)
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