Date published: 2026-5-27

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PLA1 Substrates

Santa Cruz Biotechnology now offers a broad range of PLA1 substrates for use in various applications. PLA1 substrates are specialized molecules utilized extensively in biochemical and enzymatic research to study the activity of phospholipase A1 (PLA1) enzymes. These substrates are vital in the investigation of lipid metabolism, membrane biology, and signal transduction processes. PLA1 enzymes selectively hydrolyze the sn-1 acyl bond of phospholipids, releasing fatty acids and lysophospholipids, which are critical in cellular signaling and membrane dynamics. By using PLA1 substrates, researchers can quantitatively measure enzyme activity, elucidate substrate specificity, and understand the enzyme's role in various biological systems. The ability to selectively modulate lipid composition through PLA1 activity allows for the exploration of membrane protein functions, the biophysical properties of membranes, and the intracellular trafficking of lipids. Moreover, PLA1 substrates play a crucial role in developing biochemical assays and high-throughput screening methods, facilitating the discovery of novel enzyme inhibitors or activators. These substrates are also employed in structural biology studies to reveal the enzyme-substrate interaction mechanisms at the molecular level. Santa Cruz Biotechnology provides a variety of PLA1 substrates, including synthetic analogs and naturally occurring phospholipids, tailored to meet the specific needs of researchers in diverse fields such as biochemistry, molecular biology, and cell biology. View detailed information on our available PLA1 substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

1,2-bis(Heptanoylthio)glycerophosphocholine

89019-63-6sc-201428
5 mg
$296.00
(0)

1,2-bis(Heptanoylthio)glycerophosphocholine acts as a phospholipase A1 (PLA1) substrate, exhibiting unique interactions with lipid membranes. Its structure facilitates the hydrolysis of phospholipids, leading to the release of fatty acids and lysolipids. The compound's hydrophobic heptanoyl chains enhance membrane affinity, promoting localized enzymatic activity. This specificity in lipid interactions influences cellular signaling pathways and membrane dynamics, showcasing its role in lipid metabolism.