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order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Phospholipase A2, group III (PLA2G3) belongs to a superfamily of intracellular and secreted enzymes that catalyze the hydrolysis of glycerophospholipids at the sn-2 position to release fatty acids and lysophospholipids. PLA2G3 enzymes were originally identified in invertebrates such as bees and scorpions. PLA2G3 has been shown to be a calcium dependent enzyme. It consists of a central group III sPLA2 domain flanked by unique N- and C-terminal domains that are proteolytically removed in most tissues. The sPLA2 domain is sufficient for catalytic activity. PLA2G3 is preferentially expressed in the microvascular endothelium of tissues with inflammation, ischemic injury and cancer.
References: The UniProt Consortium. Nucleic Acids Res. 47: D506-515 (2019); Nucleic Acids Res. 2016 Jan 4;44(D1):D733-45, PMID:26553804