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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:
9001-84-7
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-637-7
MDL number:
MFCD00131890
EC Number:
3.1.1.4 (BRENDA, IUBMB)
Specific activity:
≥600 units/mg protein

Key Documents

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Product Name

Phospholipase A2 from porcine pancreas, ammonium sulfate suspension, ≥600 units/mg protein

form

ammonium sulfate suspension

specific activity

≥600 units/mg protein

UniProt accession no.

P00592

storage temp.

2-8°C

Quality Level

200

Gene Information

pig ... PLA2G1B(445525)

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P8913L0382L7525
Phospholipase A2 from porcine pancreas ammonium sulfate suspension, ≥600 units/mg protein

Sigma-Aldrich

P6534

Phospholipase A2 from porcine pancreas

Phospholipase A2 from bovine pancreas lyophilized powder, ≥20 units/mg protein

Sigma-Aldrich

P8913

Phospholipase A2 from bovine pancreas

Lipase from porcine pancreas Type VI-S, ≥20,000 units/mg protein, lyophilized powder

Sigma-Aldrich

L0382

Lipase from porcine pancreas

L-Lactic Dehydrogenase from porcine heart ammonium sulfate suspension, ≥200 units/mg protein

Sigma-Aldrich

L7525

L-Lactic Dehydrogenase from porcine heart

Gene Information

pig ... PLA2G1B(445525)

Gene Information

cow ... PLA2G1B(282457)

Gene Information

-

Gene Information

pig ... LDHA(407245)

specific activity

≥600 units/mg protein

specific activity

≥20 units/mg protein

specific activity

≥20,000 units/mg protein

specific activity

≥200 units/mg protein

form

ammonium sulfate suspension

form

lyophilized powder

form

lyophilized powder

form

ammonium sulfate suspension

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

UniProt accession no.

P00592

UniProt accession no.

P00593

UniProt accession no.

-

UniProt accession no.

P00339

Quality Level

200

Quality Level

200

Quality Level

300

Quality Level

200

Analysis Note

Protein determined by biuret.

Application

Phospholipase A2 has been used in phospholipase assay and to determine rat renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation.[1][2]

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.[3]

General description

Phospholipase A2 is a small disulfide-rich protein having 124 residues.[4][5] It is a calcium-dependent enzyme.[3]

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.

Physical form

Suspension in 3.2 M (NH4)2SO4 solution, pH 5.5

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000354480
0000345855
0000354480
0000310624
0000345855

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Knut Kölbel et al.
Biophysical chemistry, 206, 12-21 (2015-06-29)
Porcine pancreatic phospholipase A2, a small and disulfide rich protein, is extremely resistant against chemically or thermally induced unfolding. Despite this marked resistance, the protein displays broad unfolding transitions resulting in comparatively low apparent thermodynamic stability. Broad unfolding transitions may
R A Zager et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(17), 8297-8301 (1993-09-01)
During hypoxic or ischemic renal tubular injury, phospholipase A2 (PLA2) induces membrane deacylation, causing fatty acid accumulation and phospholipid breakdown. Because these changes can compromise cellular integrity, PLA2 activity has been widely proposed as a critical mediator of hypoxic renal
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
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 =
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