PLA2G6
PLA2G6 (phospholipase A2 group VI) is an A2 phospholipase that catalyses the release of fatty acids from phospholipids. It is also known as iPLA2, iPLA2beta, PNPLA9, PARK14 and NBIA2, and UniProt lists it as the 85/88 kDa calcium-independent phospholipase A2. Browse Assay Genie's current range of PLA2G6 research reagents below, or read on for the biology behind the target.
PLA2G6 is an A2 phospholipase, a class of enzyme that catalyses the release of fatty acids from phospholipids. According to the NCBI Gene summary, the encoded protein may play a role in phospholipid remodelling, arachidonic acid release, leukotriene and prostaglandin synthesis, Fas-mediated apoptosis, and transmembrane ion flux in glucose-stimulated B-cells. These activities place it at the junction of membrane lipid turnover and lipid-derived signalling.
The human PLA2G6 gene is classed by HGNC within several groups: ankyrin repeat domain containing, patatin like phospholipase domain containing, phospholipases and thioester hydrolases. The enzyme is assigned EC 3.1.1.4 and is described as calcium-independent, which is reflected in the earlier gene name phospholipase A2, group VI (cytosolic, calcium-independent). UniProt records the protein in the cytoplasm, at the cell membrane, in the mitochondrion and in pseudopodia, so it is not confined to a single compartment.
Several transcript variants encoding multiple isoforms have been described, although the full-length nature of only three has been determined. The UniProt function annotation draws attention to this diversity: it describes a form that lacks the catalytic domain and may act as a negative regulator of the catalytically active isoforms. Researchers working with the PLA2G6 protein should therefore consider which isoform is relevant to their question. The gene also carries the aliases iPLA2, iPLA2beta, PNPLA9, PARK14 and NBIA2, which are useful to know when searching the literature.
PLA2G6 releases fatty acids from phospholipids and may contribute to phospholipid remodelling, making it a focus for studies of membrane lipid turnover.
The protein may take part in arachidonic acid release and in leukotriene and prostaglandin synthesis, linking it to lipid mediator research.
PLA2G6 may play a role in Fas-mediated apoptosis, so it is relevant to studies of programmed cell death pathways.
The enzyme may influence transmembrane ion flux in glucose-stimulated B-cells, which is of interest in islet cell biology.
PLA2G6 is an A2 phospholipase that catalyses the release of fatty acids from phospholipids. It may contribute to phospholipid remodelling, arachidonic acid release, leukotriene and prostaglandin synthesis, Fas-mediated apoptosis, and transmembrane ion flux in glucose-stimulated B-cells.
The gene is also called iPLA2, iPLA2beta, PNPLA9, PARK14 and NBIA2, and was previously named phospholipase A2, group VI (cytosolic, calcium-independent). Multiple transcript variants and isoforms exist; one annotated form lacks the catalytic domain and may negatively regulate the active isoforms.
Yes. Mouse and rat both have an ortholog named Pla2g6, so rodent models can be used to study the gene. Cross-species work should consider isoform differences, and you should check the datasheet of any product for its validated reactivity.
Other phospholipase A2 family members, lipid-metabolism enzymes and a related receptor with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O60733; product specifications from Assay Genie datasheets.