phospholipase

Phospholipase A2 (PLA2) is an enzyme that hydrolyzes fatty acids present in the sn-2 position of phospholipids, and is closely related to lipid metabolism and immune function.

Melittin, a small protein containing 26 amino acid residues, is the principal toxic component of bee venom. Melittin is a PLA2 activator, stimulates the activity of the low molecular weight PLA2, while it does not the increase activity of the high molecul

Anti-Inflammatory Peptide 1 Acetate (C45H82N12O14S2) possesses a potent anti-inflammatory activity in vivo and is a strong inhibitor of phospholipase A2 (PLA2), whose increased presence and activity results in inflammation and pain at certain bodily sites

Melittin TFA is a small protein containing 26 amino acid residues, is the principal toxic component of bee venom. Melittin is a PLA2 activator, stimulates the activity of the low molecular weight PLA2, while it does not the increase activity of the high m

Melittin Acetate (Forapin Acetate) is a PLA2 activator. Melittin Acetate stimulates the activity of the low molecular weight PLA2, while it does not increase the activity of the high molecular weight PLA2.

Melittin free acid, a basic 26-amino-acid polypeptide, constitutes the primary active component of honeybee venom and serves as a phospholipase A2 (PLA2) activator. Exhibiting a broad-spectrum antifungal effect, it presents MIC values ranging from 0.4-60 μM. Its mechanism includes inducing cell apoptosis, inhibiting (1,3)-β-D-glucan synthase, and engaging in multiple pathways [1] [2].

The sPLA2-IIA Inhibitor is a cyclic pentapeptide analog of FLSYK, specifically cyclic 2-Nal-Leu-Ser-2-Nal-Arg (c2), which interacts with human IIA phospholipase A2 (hGIIA) to impede its ester bond hydrolyzing function. As part of the esterase superfamily, sPLA2 enzymatically cleaves the sn-2 ester bond in glycerophospholipids, releasing arachidonic acid and lysophospholipids[1].

Endogenous peptide GPR83 agonist. ProSAAS-derived neuropeptide. Activates phospholipase C (PLC)-mediated signaling cascade in mouse hypothalamus.

Mastoparan X, a tetradecapeptide derived from wasp venom, functions as a GTP-binding regulatory protein (G protein)-activating peptide. It directly activates G proteins coupled to phospholipase C, inducing secretion in various cell types [1].

Antiflammin P2 is a nonapeptide fragment of lipocortin I which has no phospholipase A2 inhibitory and anti-inflammatory activity.