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Merck

C1907

Calcineurin from bovine brain

lyophilized powder, ≥2,500 units/mg protein

Sinónimos:

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

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Número CAS:
Número MDL:
Código UNSPSC:
51111800
NACRES:
NA.32

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origen biológico

bovine

Nivel de calidad

Formulario

lyophilized powder

actividad específica

≥2,500 units/mg protein

mol peso

dimer ~77 kDa
subunit mol wt 19-58 kDa

composición

Protein, 0.3-1.7% Lowry

solubilidad

H2O: soluble

Nº de acceso UniProt

temp. de almacenamiento

−20°C

Información sobre el gen

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1 of 4

Este artículo
208694SAB4200816539568
specific activity

≥2,500 units/mg protein

specific activity

≥250,000 units/mg protein

specific activity

-

specific activity

≥300,000 U/mg, ≥50,000 units/mL

Gene Information

cow ... PPP3CA(286852)

Gene Information

bovine ... Calm(32659)

Gene Information

bovine ... PPP3CA(286852)
human ... CALNA(5530)
rat ... Caln1(363909)

Gene Information

-

biological source

bovine

biological source

bovine brain

biological source

mouse

biological source

-

form

lyophilized powder

form

lyophilized

form

-

form

liquid

UniProt accession no.

P48452

UniProt accession no.

-

UniProt accession no.

Q08209

UniProt accession no.

-

solubility

H2O: soluble

solubility

aqueous buffer: soluble, water: soluble

solubility

-

solubility

-

Descripción general

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.[1]

Aplicación

Calcineurin from bovine brain has been used:
  • as a positive control in western blot analysis of oocytes and cumulus cells proteome[2]
  • as a positive control in calmodulin (CaM)-agarose binding assay[3]
  • to test its phosphatase activity in the presence of okadaic acid[4]

Acciones bioquímicas o fisiológicas

Calcineurin (CaN) activity is stimulated by nickel (Ni2+) and manganese (Mn2+) ions.[1] It participates in the coupling of Ca2+ signals.[1] CaN may regulate oocyte growth and meiotic maturation in porcine.[2] It also participates in gene regulation, cell survival, and death.[4]
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.
The major calmodulin-binding protein found in the brain. A key enzyme involved in T-cell activation and hyperphosphorylation of tau protein in Alzheimer′s disease.

Forma física

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

Nota de análisis

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

Otras notas

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.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves


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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
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
Calmodulin binds to and regulates the activity of beta-secretase (BACE1)
Chavez SE and O?Day DH
Current research journal of biological sciences, 1, 37-47 (2007)
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

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