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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

以硫酸铵悬浮液形式提供的酶的使用指南

Instructions for working with enzymes supplied as ammonium sulfate suspensions


B van den Berg et al.
The EMBO journal, 14(17), 4123-4131 (1995-09-01)
The lipolytic enzyme phospholipase A2 (PLA2) is involved in the degradation of high-molecular weight phospholipid aggregates in vivo. The enzyme has very high catalytic activities on aggregated substrates compared with monomeric substrates, a phenomenon called interfacial activation. Crystal structures of
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
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



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