Recombinant Human LYPLAL1 protein is a Human Full Length protein, in the 1 to 237 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
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Palmitoyl thioesterase that catalyzes depalmitoylation of CGAS and KCNMA1 (PubMed:22052940, PubMed:22399288, PubMed:37802025). Acts as a regulator of innate immunity by mediating depalmitoylation of CGAS, thereby preventing CGAS homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025). Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site (PubMed:22052940).
Lysophospholipase-like protein 1, LYPLAL1
Recombinant Human LYPLAL1 protein is a Human Full Length protein, in the 1 to 237 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl
ab130056 is purified using conventional chromatography techniques.
Palmitoyl thioesterase that catalyzes depalmitoylation of CGAS and KCNMA1 (PubMed:22052940, PubMed:22399288, PubMed:37802025). Acts as a regulator of innate immunity by mediating depalmitoylation of CGAS, thereby preventing CGAS homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025). Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site (PubMed:22052940).
Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.
LYPLAL1 also known as Lysophospholipase-like 1 is a protein involved in metabolic processes and has an approximate molecular mass of 31 kDa. This protein is expressed in various tissues with substantial levels found in adipose tissue and the liver. LYPLAL1 shows similarity to lysophospholipase enzymes but lacks the capacity to carry out specific functions typical of those enzymes. Instead LYPLAL1 contributes mechanically by modifying certain lipid molecules impacting lipid metabolism.
Lysophospholipase-like 1 influences fat storage and energy homeostasis within cells. It does not function alone but rather interacts potentially with other enzymes to regulate these processes. While LYPLAL1 itself is not part of a large complex it operates in an environment with various lipid-related enzymes that jointly maintain lipid balance in the body. Its activity can affect the breakdown of triglycerides and might have roles in metabolic regulation and efficiency.
LYPLAL1 integrates into lipid metabolic pathways notably lipid biosynthesis and lipid degradation. These pathways are central in balancing energy supply through the manipulation and storage of lipid molecules. Through these metabolic pathways LYPLAL1 may have connections with proteins such as hormone-sensitive lipase (HSL) which plays a significant role in lipid mobilization and perilipin which modulates lipid droplet storage. The regulation and interaction with these proteins affirm LYPLAL1's place in lipid metabolism.
Variations in LYPLAL1 activity or expression have links with obesity and type 2 diabetes. The gene coding for LYPLAL1 has associations with variations impacting body mass index (BMI) and fat distribution which are critical factors in these metabolic disorders. Connections with other proteins like adiponectin which plays an important role in glucose regulation and fatty acid oxidation strengthen LYPLAL1’s involvement in these diseases. Understanding the relationship of LYPLAL1 to these conditions offers new insights into metabolic health management strategies.
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15% SDS-PAGE showing ab130056 (3μg).
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