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C1907

Sigma-Aldrich

钙调磷酸酶 来源于牛大脑

lyophilized powder, ≥2,500 units/mg protein

别名:

PP2B, 磷蛋白磷酸水解酶, 蛋白磷酸酶 2B, 调节因子结合蛋白, 钙/钙调素活化的蛋白磷酸酶, 钙调素结合蛋白

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About This Item

CAS号:
90371-51-0
MDL號碼:
MFCD00130697
分類程式碼代碼:
51111800
NACRES:
NA.32

生物源

bovine

品質等級

200

形狀

lyophilized powder

比活性

≥2,500 units/mg protein

分子量

dimer ~77 kDa
subunit mol wt 19-58 kDa

成份

Protein, 0.3-1.7% Lowry

溶解度

H2O: soluble

UniProt登錄號

P48452

儲存溫度

−20°C

基因資訊

cow ... PPP3CA(286852)

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一般說明

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.

應用

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

生化／生理作用

钙调磷酸酶是一种环孢菌素敏感、钙调节的丝氨酸-苏氨酸蛋白质磷酸酶，具有较广的底物特异性。它是大脑中发现的主要钙调素结合蛋白。最早鉴定为一种磷酸二酯酶 3′:5′ 环核苷酸 (PDE) 的钙调素活化抑制剂，钙调磷酸酶对腺苷酸环化酶具有类似的作用。是与 T 细胞活化相关的关键酶。也与阿尔茨海默病中 τ 蛋白的过磷酸化有关，并且已显示出可阻碍分化型 PC12 细胞中 τ 蛋白进行钙蛋白酶介导的蛋白质水解的特性。
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.

單位定義

当与两单位活化剂 (P 2277) 以及 0.1mM Ca2+ 置于酶偶联系统中分析时，在 pH 7.5 和 30°C 下，一单位本品可以对活化的磷酸二酯酶 3′:5′-环核苷酸 (P 9529) 造成 50% 的抑制。

外觀

冻干粉，含 0.5% EGTA，缓冲盐及稳定剂。

分析報告

Sigma 在含 65mM KCl、8mM MgSO4 以及 0.3% 白蛋白且 pH 为 7.5 的 80mM Tris 中测试了其活性。

儲存類別代碼

11 - Combustible Solids

水污染物質分類（WGK）

WGK 2

閃點（°F）

Not applicable

閃點（°C）

Not applicable

個人防護裝備

Eyeshields, Gloves

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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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