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C1907

Sigma-Aldrich

Calcineurin from bovine brain

lyophilized powder, ≥2,500 units/mg protein

Synonyme(s) :

Calcium/Calmodulin-Activated Protein Phosphatase, Calmodulin binding protein, Modulator binding protein, PP2B, Phosphoprotein Phosphohydrolase, Protein phosphatase 2B

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About This Item

Numéro CAS:
90371-51-0
Numéro MDL:
MFCD00130697
Code UNSPSC :
51111800
Nomenclature NACRES :
NA.32

Source biologique

bovine

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

≥2,500 units/mg protein

Poids mol.

dimer ~77 kDa
subunit mol wt 19-58 kDa

Composition

Protein, 0.3-1.7% Lowry

Solubilité

H2O: soluble

Numéro d'accès UniProt

P48452

Température de stockage

−20°C

Informations sur le gène

cow ... PPP3CA(286852)

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Description générale

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.

Application

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Forme physique

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

Remarque sur l'analyse

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
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
C B Klee et al.
Biochemistry, 17(1), 120-126 (1978-01-10)
The Ca2+-dependent, reversible, interaction of cyclic adenosine 3',5'-monophosphate (cAMP) phosphodiesterase with its activator has been used to purify the enzyme by affinity chromatography. Activator-dependent cAMP phosphodiesterase is only a minor component of the proteins specifically adsorbed in the presence of
C X Gong et al.
Brain research, 741(1-2), 95-102 (1996-11-25)
Abnormally hyperphosphorylated tau is the major protein component of neurofibrillary tangles, the characteristic lesion of Alzheimer's disease (AD). Protein phosphatases (PP) type 1 (PP-1), type 2A (PP-2A) and type 2B (PP-2B) appear to be involved in the regulation of tau
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