Phospholipase A2, Crotalus adamanteus Venom
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Phospholipase A2 (PLA2), Crotalus adamanteus Venom is a membrane phospholipid-targeting enzyme. Phospholipase A2, Crotalus adamanteus catalyzes cleavage of the sn-2-acyl bond of membrane phospholipids, producing lysophospholipids and free fatty acids. Phospholipase A2, Crotalus adamanteus Venom can be used for biochemical research.
For research use only. We do not sell to patients.
- CAS No.: 9001-84-7
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Storage:
Please store the product under the recommended conditions in the Certificate of Analysis.
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Biological Activity
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Chemical Information
- Purity & Documentation
- References
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Help & FAQs
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Biological Activity
Phospholipase A2, Crotalus adamanteus Venom is a stable, calcium2+-dependent enzyme with preferential activity toward aggregated phospholipid substrates[1].
Phospholipase A2, Crotalus adamanteus Venom is inhibited by a broad range of compounds acting through multiple mechanisms, including interface disruption, calcium modulation, non-specific binding, and covalent enzyme modification[1].
Phospholipase A2, Crotalus adamanteus Venom activity is inhibited by kaempferol, quercetin, myricetin, and vitamin E, while flavanones with a reduced C-ring 2-3 double bond show diminished inhibitory activity against this enzyme[4].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
Chemical Information
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CAS No. 9001-84-7
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Appearance Solid
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Color White to off-white
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SMILES
[Phospholipase A2, Crotalus adamanteus Venom]
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Synonyms
PLA2, Crotalus adamanteus Venom
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Please store the product under the recommended conditions in the Certificate of Analysis.
Purity & Documentation
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Data Sheet (264 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
References
[1]. Chang J, et al. Phospholipase A2: function and pharmacological regulation. Biochem Pharmacol. 1987 Aug 1;36(15):2429-36. [Content Brief]
[2]. Grass DS, et al. Expression of human group II PLA2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate. J Clin Invest. 1996 May 15;97(10):2233-41. [Content Brief]
[4]. Nanda BL, Nataraju A, Rajesh R, et al.. PLA2 mediated arachidonate free radicals: PLA2 inhibition and neutralization of free radicals by anti-oxidants--a new role as anti-inflammatory molecule. Current topics in medicinal chemistry. 2007;7(8):765-77. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Phospholipase A2, Crotalus adamanteus Venom Related Classifications
HY-P3029A Related Classifications
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- Phospholipase A2, Crotalus adamanteus Venom
- 9001-84-7
- PLA2, Crotalus adamanteus Venom
- Phospholipase
- free fatty acids
- quercetin
- kaempferol
- Phospholipase A2
- neuromuscular junction
- lysophosphatidylcholine
- phosphatidylcholine
- lysophospholipids
- Crotalus adamanteus Venom
- membrane phospholipids
- Inhibitor
- inhibitor
- inhibit