Explore HT
Gene
PLAAT5
Uniprot
Q96KN8
Protein
Phospholipase A and acyltransferase 5
See alternative names Ca(2+)-independent N-acyltransferase,
H-rev107-like protein 5,
HRAS-like suppressor 5
Uniprot Function Description
Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:22825852, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:22825852). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19000777, PubMed:22825852).
Sample type
Recommended sample types are human plasma and serum. For other sample types e.g cerebrospinal fluid, (CSF), tissue or cell lysate, please contact support@olink.com for more information. Please note that protein expression levels are expected to vary in different sample types and certain assays may be affected by interfering substances such as hemolysate.
Precision
Precision (repeatability) is calculated from linearized NPX values over LOD.
Analytical measuring range
The technical data reported below refers to the measured value in the in vitro validation assays run using known concentrations of recombinant antigen.
Dilution factor
For optimal assay readout, Olink assays are run using different dilutions of the original samples e.g. undiluted, 1:10, or higher. The dilution factor for this assay is noted below and should be taken into account when estimating the appropriate addressable biological concentration of the protein based on the in vitro validation data.
Biomarker Validation Data
Additional validation data, as well as a more detailed description of how the Olink panels are quality controlled can be found in our Data Validation documents – go to Document download center