PLA2R1 (human) full length protein-synthetic nanodisc

Discover a breakthrough in membrane protein research and drug development with DIMA Biotech's Synthetic Nanodiscs. Traditional methods struggle with challenges in obtaining water-soluble and bioactive forms of multi-transmembrane proteins. Our innovative polymer-based Nanodisc platform offers a game-changing solution by excluding membrane scaffold proteins (MSPs), resulting in a cleaner system with fewer interferences for downstream assays. By disassembling cell membranes into nanoscale disc-shaped structures, our technology enables the purification of membrane proteins to high homogeneity under aqueous conditions. Explore how Synthetic Nanodiscs empower the functional characterization of multi-span transmembrane proteins in their active form, revolutionizing the future of membrane protein research and drug development. Protein function: Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2- IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B (PubMed:15611272, PubMed:7721806). In podocytes, binding of sPLA2-IB/PLA2G1B can regulate podocyte survival and glomerular homeostasis (PubMed:25335547). [The UniProt Consortium]