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Merck

C1907

Sigma-Aldrich

Calcineurin aus Rinderhirn

lyophilized powder, ≥2,500 units/mg protein

Synonym(e):

Calmodulin-bindendes Protein

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About This Item

CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
51111800
NACRES:
NA.32

Biologische Quelle

bovine

Qualitätsniveau

Form

lyophilized powder

Spezifische Aktivität

≥2,500 units/mg protein

Mol-Gew.

dimer ~77 kDa
subunit mol wt 19-58 kDa

Zusammensetzung

Protein, 0.3-1.7% Lowry

Löslichkeit

H2O: soluble

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

Angaben zum Gen

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Allgemeine Beschreibung

Calcineurin (CaN) comprises CaN A and CaN B subunits. It exists as a heterodimer with a calmodulin-binding domain, catalytic site, a CaN B binding domain, and an autoinhibitory domain.

Anwendung

Calcineurin from bovine brain has been used:
  • as a positive control in western blot analysis of oocytes and cumulus cells proteome
  • as a positive control in calmodulin (CaM)-agarose binding assay
  • to test its phosphatase activity in the presence of okadaic acid

Biochem./physiol. Wirkung

Calcineurin (CaN) activity is stimulated by nickel (Ni2+) and manganese (Mn2+) ions. It participates in the coupling of Ca2+ signals. CaN may regulate oocyte growth and meiotic maturation in porcine. It also participates in gene regulation, cell survival, and death.
Calcineurin is a cyclosporin-sensitive, calcium-regulated, serine-threonine protein phosphatase with broad substrate specificity. It is the major calmodulin-binding protein found in the brain. First identified as an inhibitor of the calmodulin activation of phosphodiesterase 3′:5′ cyclic nucleotide (PDE), calcineurin has similar effects on adenylate cyclase. Serves as a key enzyme involved in T-cell activation. Also involved in the hyperphosphorylation of tau protein in Alzheimer′s disease and has been shown to prevent calpain-mediated proteolysis of tau in differentiated PC12 cells.

Einheitendefinition

One unit will cause a 50% inhibition of the activated phosphodiesterase, 3′:5′-cyclic nucleotide (P 9529) activity when assayed with two units of activator (P 2277) and 0.1 mM Ca2+ in an enzyme coupled system at pH 7.5 at 30 °C.

Physikalische Form

Lyophilized powder containing 0.5% EGTA, buffer salts and stabilizers.

Hinweis zur Analyse

Sigma tests activity in 80 mM Tris, pH 7.5 with 65 mM KCl, 8 mM MgSO4 and 0.3% albumin.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves


Analysenzertifikate (COA)

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Lenka Tůmová et al.
Animal reproduction science, 141(3-4), 154-163 (2013-08-27)
The processes of oocyte growth, acquisition of meiotic competence and meiotic maturation are regulated by a large number of molecules. One of them could be calcineurin consisting of catalytic subunit A (Aα, Aβ, Aγ isoforms) and regulatory subunit B (B1
Felicia Ranta et al.
Cellular signalling, 20(10), 1780-1786 (2008-07-10)
Previously, we described that apoptotic cell death induced by the synthetic glucocorticoid dexamethasone (dex) is inhibited by calcineurin inhibitors, FK506 and deltamethrin, in insulin-secreting cells. The aim of the present study was to examine the mechanism of dex-dependent activation of
H Q Xie et al.
Journal of neuroscience research, 53(2), 153-164 (1998-07-22)
The effects of calcium influx on tau levels and phosphorylation were examined in differentiated PC12 cells. Maitotoxin-induced calcium influx resulted in time- and concentration-dependent tau dephosphorylation and degradation. Incubation of PC12 cells with a membrane-permeable calpain inhibitor blocked maitotoxin-induced tau
Modulator binding protein. Bovine brain protein exhibiting the Ca2+-dependent association with the protein modulator of cyclic nucleotide phosphodiesterase.
J H Wang et al.
The Journal of biological chemistry, 252(12), 4175-4184 (1977-06-25)
Ashakumary Lakshmikuttyamma et al.
Neurochemical research, 29(10), 1913-1921 (2004-11-10)
A major cause of neuronal dysfunction is due to altered Ca2+ regulation. An increase in Ca2+ influx can activate Ca2+-dependent enzymes including calpains, causing the proteolysis of its specific substrates. In the present study, calcineurin (CaN) was found to be

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