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P1431

Sigma-Aldrich

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

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

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

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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.

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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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)
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
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
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

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