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Merck
CN

P6534

磷脂酶 A2 来源于猪胰腺

ammonium sulfate suspension, ≥600 units/mg protein

别名:

PLA, 卵磷脂酶 A, 磷脂酰胆碱 2-酰基水解酶

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-637-7
MDL number:
Specific activity:
≥600 units/mg protein
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form

ammonium sulfate suspension

Quality Level

specific activity

≥600 units/mg protein

UniProt accession no.

storage temp.

2-8°C

Gene Information

General description

磷脂酶 A2 是一种富含二硫键的小分子蛋白,有 124 个残基。 是一种钙依赖性酶。

Application

磷脂酶 A2 已用于磷脂酶试验,并确定大鼠肾近曲小管段 (PTS) 在氧合和缺氧-复氧过程中的活性。

Biochem/physiol Actions

与单体底物相比,它对聚集的底物具有较高的催化活性。
水解 β-两性甘油磷脂的酯键。首选底物为磷脂酰胆碱、磷脂酰乙醇胺及其缩醛磷脂类似物。磷脂酰肌醇和磷脂酰丝氨酸也被水解。其会攻击完整细胞膜上的磷脂。

Physical form

在 3.2 M (NH 4 ) 2 SO 4 溶液 (pH 5.5) 中的混悬液

Analysis Note

双缩脲法测定蛋白质。

Other Notes

在 pH 8.0、37°C 条件下,1 个单位每分钟将 1.0 μmol 大豆 L-α-磷脂酰胆碱水解为 L-α-溶血磷脂酰胆碱和 1 个脂肪酸。


存储类别

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

低风险生物材料

此项目有



历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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商品

Instructions for working with enzymes supplied as ammonium sulfate suspensions

以硫酸铵悬浮液形式提供的酶的使用指南

相关内容


A A Grippo et al.
Journal of reproduction and fertility, 102(1), 87-93 (1994-09-01)
Cholesterol and phospholipid concentrations and phospholipase activity were measured in fluid from cannulae collected from the bovine oviductal isthmus and ampulla at different stages of the oestrous cycle. The cholesterol concentration and cholesterol normalized by protein were significantly (P =
B van den Berg et al.
Journal of biomolecular NMR, 5(2), 110-121 (1995-02-01)
The three-dimensional structure of porcine pancreatic PLA2 (PLA2), present in a 40 kDa ternary complex with micelles and a competitive inhibitor, has been determined using multidimensional heteronuclear NMR spectroscopy. The structure of the protein (124 residues) is based on 1854
Elena Venuti et al.
Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society, 16(6), 763-770 (2017-07-26)
Bile salt stimulated lipase (BSSL; Enzyme Commission (EC) number 3.1.1.13) has been a candidate triglyceridase for improving enzyme therapy for pancreatic insufficiency; however, its efficacy is near absent. We hypothesise that similarly to pancreatic lipase, BSSL is inhibited by phospholipids



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