P6534
Phospholipase A2 from porcine pancreas
ammonium sulfate suspension, ≥600 units/mg protein
Synonym(s):
Lecithinase A, PLA2, Phosphatidylcholine 2-acylhydrolase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-637-7
MDL number:
Specific activity:
≥600 units/mg protein
form
ammonium sulfate suspension
Quality Level
specific activity
≥600 units/mg protein
UniProt accession no.
storage temp.
2-8°C
Gene Information
pig ... PLA2G1B(445525)
General description
Phospholipase A2 is a small disulfide-rich protein having 124 residues. It is a calcium-dependent enzyme.
Application
Phospholipase A2 has been used in phospholipase assay and to determine rat renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation.
Biochem/physiol Actions
Hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. Aggressively attacks phospholipids in membranes of intact cells.
It has a high catalytic activity on aggregated substrates compared to monomeric substrates.
Physical form
Suspension in 3.2 M (NH4)2SO4 solution, pH 5.5
Analysis Note
Protein determined by biuret.
Other Notes
One unit will hydrolyze 1.0 μmole of soybean L-α-phosphatidylcholine to L-α-lysophosphatidylcholine and a fatty acid per min at pH 8.0 at 37 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
低风险生物材料
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Articles
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
Related Content
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| P6534-10MG | 04061833273708 |
| P6534-1MG | 04061826683811 |
| P6534-5MG | 04061833273715 |