P9279
Phospholipase A2 from honey bee venom (Apis mellifera)
salt-free, lyophilized powder, 600-2400 units/mg protein
Synonym(s):
Lecithinase A, PLA2, Phosphatidylcholine 2-acylhydrolase
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About This Item
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form
salt-free, lyophilized powder
Quality Level
specific activity
600-2400 units/mg protein
mol wt
14.5 kDa
UniProt accession no.
storage temp.
−20°C
Gene Information
honey bee ... Pla2(406141)
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General description
Phospholipase A2 from honey bee venom (Apis mellifera) is a calcium-dependent lipolytic enzyme.
Application
Phospholipase A2 from honey bee venom (Apis mellifera) has been used
- to determine renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation
- in the treatment of photosystem-II (PSII) dimer complex of Synechocystis to study changes in oxygen-evolving activity
- as a standard in phospholipase activity assay
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.
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 8.9 at 25 °C.
Analysis Note
Protein determined by biuret.
inhibitor
Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Third calcium ion found in an inhibitor-bound phospholipase A2.
Sekar K
Acta Crystallographica Section D, Biological Crystallography, 62, 392-397 (2006)
Lipids in oxygen-evolving photosystem II complexes of cyanobacteria and higher plants.
Sakurai I
Journal of Biochemistry, 140(2), 201-209 (2006)
Milleporin-1, a new phospholipase A2 active protein from the fire coral Millepora platyphylla nematocysts.
Radwan FF and Aboul-Dahab HM
Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP, 139(4), 267-272 (2004)
Phospholipase A2 activity can protect renal tubules from oxygen deprivation injury.
Zager RA
Proceedings of the National Academy of Sciences of the USA, 90(17), 8297-8301 (1993)
Ming Chen et al.
Scientific reports, 7(1), 15931-15931 (2017-11-23)
Hepatitis C virus (HCV), dengue virus (DENV) and Japanese encephalitis virus (JEV) belong to the family Flaviviridae. Their viral particles have the envelope composed of viral proteins and a lipid bilayer acquired from budding through the endoplasmic reticulum (ER). The
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