PLA1A
PLA1A (phospholipase A1 member A, also known as ps-PLA1) is a secreted phospholipase that removes fatty acids from the sn-1 position of phosphatidylserine and its lysophospholipid derivative. It belongs to the lipase family within the AB hydrolase superfamily. Browse Assay Genie's current range of PLA1A research reagents below, or read on for the biology behind the target.
PLA1A is a phospholipase that hydrolyses fatty acids at the sn-1 position of phosphatidylserine (PS) and 1-acyl-2-lysophosphatidylserine (lyso-PS). The secreted enzyme hydrolyses phosphatidylserine in liposomes. UniProt annotates its activity as acting on lyso-PS but not on PS, so the substrate preference is worth checking against the assay system you use. Because the enzyme is secreted, it acts outside the cell rather than within an intracellular compartment.
The PLA1A gene encodes a protein of the AB hydrolase superfamily, in the lipase family. HGNC places it in the phospholipases gene group. The enzyme carries the EC number 3.1.1.111. The human gene has mouse and rat orthologs, both named Pla1a, which allows comparative work in rodent models. Researchers looking for a PLA1A antibody, PLA1A ELISA kit or recombinant PLA1A protein are usually interested in this secreted lipid-modifying enzyme and in how it handles phosphatidylserine and lysophosphatidylserine.
Three transcript variants encoding different isoforms have been reported for the PLA1A gene according to the RefSeq summary. The alias ps-PLA1 reflects its phosphatidylserine-specific phospholipase A1 activity. Related phospholipase families, such as the phospholipase A2 group, act on the sn-2 position of phospholipids and are distinct from this sn-1-acting enzyme.
PLA1A cleaves the sn-1 fatty acid from phosphatidylserine and lysophosphatidylserine, making it a useful enzyme for studying phospholipid turnover.
UniProt annotates PLA1A as hydrolysing lyso-PS but not PS, so it is relevant to work on lysophospholipid handling.
As a member of the AB hydrolase superfamily lipase family, PLA1A serves as a model for secreted lipase function and substrate specificity.
PLA1A acts extracellularly and hydrolyses phosphatidylserine in liposomes, supporting work on secreted lipid-modifying enzymes.
PLA1A is a secreted phospholipase that hydrolyses fatty acids at the sn-1 position of phosphatidylserine and 1-acyl-2-lysophosphatidylserine. It hydrolyses phosphatidylserine in liposomes, while UniProt notes activity on lyso-PS but not PS. Its EC number is 3.1.1.111.
PLA1A is also known as ps-PLA1, and its full name is phospholipase A1 member A. HGNC lists no previous symbols or names. According to the RefSeq summary, three transcript variants encoding different isoforms have been found for the gene.
Yes, mouse and rat both have an ortholog named Pla1a, so rodent models can be used to study the enzyme. Cross-species work should be planned carefully; check the datasheet of any product for its validated reactivity.
Other phospholipases, including members of the phospholipase A2 group, and related lipid-metabolism targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q53H76; product specifications from Assay Genie datasheets.