Recombinant Mouse Lysophospholipase 1/LPL-I protein
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Recombinant Mouse Lysophospholipase 1/LPL-I protein is a Mouse Full Length protein, in the 1 to 230 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
Apt1, Pla1a, Lypla1, Acyl-protein thioesterase 1, APT-1, Lysophospholipase 1, Lysophospholipase I, Palmitoyl-protein hydrolase, LPL-I, LysoPLA I
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Mouse Lysophospholipase 1/LPL-I protein (AB101156)
15% SDS-PAGE showing ab101156 at approximately 26.8 kDa (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Lysophospholipase 1 plays a role in maintaining lipid homeostasis. It does not function as part of a larger protein complex acting independently in the regulation of lipid turnover. By breaking down lysophospholipids the enzyme helps balance the cellular lipid composition ensuring proper membrane integrity and cellular signaling. This regulation is critical in tissues that have high turnover of lipids like the brain and liver.
Pathways
Lysophospholipase 1 participates in lipid metabolism and glycerophospholipid biosynthesis pathways. The enzyme helps process intermediates in these pathways facilitating energy production and phospholipid remodeling. In terms of related proteins LPL-I functions in coordination with phospholipase A2 in lipid degradation and this relationship impacts the synthesis of bioactive lipid mediators.
Specifications
Form
Liquid
Additional notes
ab101156 is purified using conventional chromatography techniques.
General info
Function
Acts as an acyl-protein thioesterase (By similarity). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1 (By similarity). Acts as a negative regulator of autophagy by mediating palmitoylation of SQSTM1, decreasing affinity between SQSTM1 and ATG8 proteins and recruitment of ubiquitinated cargo proteins to autophagosomes (By similarity). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (By similarity). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS) (PubMed : 9139730). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity).
Sequence similarities
Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.
Subcellular localisation
Nucleus membrane
Target data
Product promise
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