P1431
Calmodulin from bovine testes
BioUltra, ≥98% (SDS-PAGE), lyophilized powder, essentially salt free
Synonym(s):
CaM, Phosphodiesterase 3′:5′-cyclic nucleotide activator
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About This Item
Form:
lyophilized powder
Assay:
≥98% (SDS-PAGE)
Biological source:
bovine testis
Mol wt:
16.79 kDa
biological source
bovine testis
Quality Level
product line
BioUltra
assay
≥98% (SDS-PAGE)
form
lyophilized powder
mol wt
16.79 kDa
storage condition
(Keep container tightly closed in a dry and well-ventilated place)
technique(s)
ligand binding assay: suitable
impurities
salt, essentially free
UniProt accession no.
application(s)
cell analysis
storage temp.
−20°C
Gene Information
cow ... CALM3(520277)
General description
Research area: Cell Signaling
Calmodulin (CaM) is a Ca2+-sensor protein containing four EF-hand motifs that bind to four Ca2+ ions. It is found ubiquitously in all eukaryotes.
Calmodulin (CaM) is a Ca2+-sensor protein containing four EF-hand motifs that bind to four Ca2+ ions. It is found ubiquitously in all eukaryotes.
Application
Calmodulin from bovine testes has been used:
- as a component of the reaction mixture in PhosphoSens assay to measure Ca2+/calmodulin-dependent protein kinase II α (CaMKIIα) substrate phosphorylation
- to generate standard curve for the determination of in situ calmodulin concentration in tissues
- as a ligand in radio-ligand binding for studying calmodulin affinity
Biochem/physiol Actions
Calmodulin (CaM) aids in the Ca2+ signal transduction pathway in higher plants and animals. Ca2+ binding is required for CaM activation. Upon activation, CaM binds and activates numerous target proteins involved in a variety of cellular processes including regulation of plant metabolism, phytohormone signaling, ion transport, protein folding, protein phosphorylation and dephosphorylation, cell motility, exocytosis, and cytoskeletal assembly. In neurons, calcium-activated CaM helps in the regulation of glutamate receptors, modulation of proteins in signaling pathways, and regulation of voltage-gated calcium channels (VGCCs) activity.
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Related Content
QC Methods
The diversity of calcium sensor proteins in the regulation of neuronal function
McCue HV, et al.
Cold Spring Harbor Perspectives in Biology, 2(8) (2010)
Nane Griem-Krey et al.
Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 156, 113895-113895 (2022-10-25)
Ca2+/calmodulin-dependent protein kinase II alpha (CaMKIIα) is a potential target for acute neuroprotection due to its key role in physiological and pathological glutamate signaling. The hub domain organizes the CaMKII holoenzyme into large oligomers, and additional functional effects on holoenzyme
E J McConnell et al.
Circulation research, 86(2), 191-197 (2000-02-10)
Plasma membrane (Ca(2+)+Mg(2+))-ATPase and Ca(2+) transport activities, best characterized in human erythrocytes, are stimulated by calmodulin and thought to play a crucial role in the termination of cellular Ca(2+) signaling in all cells. In plasma membranes isolated from cultured porcine