Phospholipase A2 from porcine pancreas

ammonium sulfate suspension, ≥600 units/mg protein

PLA2, Phosphatidylcholine 2-acylhydrolase, Lecithinase A
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
Pricing and availability is not currently available.

Quality Level


ammonium sulfate suspension

specific activity

≥600 units/mg protein

storage temp.


Gene Information

pig ... PLA2G1B(445525)

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General description

Phospholipase A2 is a small disulfide-rich protein having 124 residues. It is a calcium-dependent enzyme.


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


1, 5, 10 mg in glass bottle

Biochem/physiol Actions

It has a high catalytic activity on aggregated substrates compared to monomeric substrates.
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.

Unit Definition

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

Analysis Note

Protein determined by biuret.


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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...
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 =...
Diethard R L Monbaliu et al.
The Journal of surgical research, 151(1), 125-131 (2008-05-13)
Secretory phospholipase A(2) (sPLA(2)) degrades cell membrane phospholipids and plays an important role in the synthesis of pro-inflammatory lipid mediators (arachidonic acid and cytokines) during inflammatory events such as ischemia-reperfusion injury after liver transplantation (LTx). A role for sPLA(2) in...
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...
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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