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Merck

P1431

Calmodulin from bovine testes

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

Sinonimo/i:

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

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Informazioni su questo articolo

Numero CAS:
77107-46-1
UNSPSC Code:
12352202
NACRES:
NA.61
MDL number:
MFCD00131869
Form:
lyophilized powder
Assay:
≥98% (SDS-PAGE)
Biological source:
bovine testis
Mol wt:
16.79 kDa

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biological source

bovine testis

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.

P62157

application(s)

cell analysis

storage temp.

−20°C

Quality Level

200

Gene Information

cow ... CALM3(520277)

Categorie correlate

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Questo articolo
P0270M1891C4874
Calmodulin from bovine testes BioUltra, ≥98% (SDS-PAGE), lyophilized powder, essentially salt free

Sigma-Aldrich

P1431

Calmodulin from bovine testes

Calmodulin from bovine heart lyophilized powder, 2,500-10,000 units/mg protein

Sigma-Aldrich

P0270

Calmodulin from bovine heart

Myelin Basic Protein bovine ≥90% (SDS-PAGE), lyophilized powder, suitable for activity assay

Sigma-Aldrich

M1891

Myelin Basic Protein bovine

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

Sigma-Aldrich

C4874

Calmodulin bovine

biological source

bovine testis

biological source

bovine heart

biological source

bovine

biological source

bovine

technique(s)

ligand binding assay: suitable

technique(s)

calcium flux assay: suitable

technique(s)

activity assay: suitable

technique(s)

-

assay

≥98% (SDS-PAGE)

assay

-

assay

≥90% (SDS-PAGE)

assay

≥98% (SDS-PAGE)

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

16.79 kDa

mol wt

-

mol wt

18.4 kDa

mol wt

Mw 19000.9 by amino acid sequence

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

Research area: Cell Signaling

Calmodulin (CaM) is a Ca2+-sensor protein containing four EF-hand motifs that bind to four Ca2+ ions.[1] It is found ubiquitously in all eukaryotes.[2]

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[3]
  • to generate standard curve for the determination of in situ calmodulin concentration in tissues[4]
  • as a ligand in radio-ligand binding for studying calmodulin affinity[5]

Biochem/physiol Actions

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 (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[1], 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.[2]

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Classe di stoccaggio

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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Certificati d'analisi (COA)

Lot/Batch Number
0000540530
0000521152
0000540530
0000521152
SLCQ6091

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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
comparative proteomics illustrates the molecular mechanism of potato (Solanum tuberosum L.) tuberization inhibited by exogenous gibberellins in vitro
Cheng L, et al.
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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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