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Merck
CN

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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化学文摘社编号:
MDL编号:
UNSPSC代码:
51111800
NACRES:
NA.32
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生物来源

bovine

质量水平

表单

lyophilized powder

比活

≥2,500 units/mg protein

分子量

dimer ~77 kDa
subunit mol wt 19-58 kDa

组成

Protein, 0.3-1.7% Lowry

溶解性

H2O: soluble

UniProt登记号

储存温度

−20°C

基因信息

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一般描述

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.

应用

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

大脑中发现的主要钙调素结合蛋白。与 T 细胞活化和阿尔茨海默病中 τ 蛋白的过磷酸化有关的关键酶。
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.

外形

冻干粉,含 0.5% EGTA,缓冲盐及稳定剂。

分析说明

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。

其他说明

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。

储存分类代码

11 - Combustible Solids

WGK

WGK 2

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves

法规信息

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分析证书(COA)

Lot/Batch Number

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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
T D Batiuk et al.
The Journal of clinical investigation, 100(7), 1894-1901 (1997-10-06)
Cyclosporine (CsA) is both a clinical immunosuppressive drug and a probe to dissect intracellular signaling pathways. In vitro, CsA inhibits lymphocyte gene activation by inhibiting the phosphatase activity of calcineurin (CN). In clinical use, CsA treatment inhibits 50-75% of CN
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
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

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