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Merck

P1431

Sigma-Aldrich

Calmodulin from bovine testes

BioUltra, ≥98% (SDS-PAGE), lyophilized powder, essentially salt free

Sinónimos:

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

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About This Item

Número de CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.61

origen biológico

bovine testis

Nivel de calidad

Línea del producto

BioUltra

Ensayo

≥98% (SDS-PAGE)

Formulario

lyophilized powder

mol peso

16.79 kDa

condiciones de almacenamiento

(Keep container tightly closed in a dry and well-ventilated place)

técnicas

ligand binding assay: suitable

impurezas

salt, essentially free

Nº de acceso UniProt

aplicaciones

cell analysis

temp. de almacenamiento

−20°C

Información sobre el gen

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Descripción general

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.

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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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)
comparative proteomics illustrates the molecular mechanism of potato (Solanum tuberosum L.) tuberization inhibited by exogenous gibberellins in vitro
Cheng L, et al.
Physiologia Plantarum, 163, 103-123 (2018)
Arkadiusz Miazek et al.
Scientific reports, 11(1), 7312-7312 (2021-04-02)
The neuronal membrane-associated periodic spectrin skeleton (MPS) contributes to neuronal development, remodeling, and organization. Post-translational modifications impinge on spectrin, the major component of the MPS, but their role remains poorly understood. One modification targeting spectrin is cleavage by calpains, a
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
Elisha R Injeti et al.
American journal of physiology. Heart and circulatory physiology, 295(6), H2289-H2298 (2008-10-07)
Postnatal decreases in vascular reactivity involve decreases in the thick filament component of myofilament calcium sensitivity, which is measured as the relationship between cytosolic calcium concentration and myosin light chain (MLC20) phosphorylation. The present study tests the hypothesis that downregulation

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