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Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. Additionally we are shipping Lysophospholipase I Antibodies (59) and Lysophospholipase I Proteins (22) and many more products for this protein.
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Data indicate that thioesterases APT1 (show FAS ELISA Kits)/APT2 (show TAP2 ELISA Kits) depalmitoylate nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2 (show NMNAT2 ELISA Kits)) and zDHHC17 is the strongest candidate palmitoyltransferase for NMNAT2 (show NMNAT2 ELISA Kits).
Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 (show LYPLA2 ELISA Kits) with that of proto-oncogene (show RAB1A ELISA Kits) H-ras (show HRAS ELISA Kits) product and growth-associated protein-43 (show GAP43 ELISA Kits)
Here, we describe the conserved functions of APT1 (show FAS ELISA Kits) and APT2 (show TAP2 ELISA Kits) across organisms and discuss the possibility that these enzymes are members of a larger family of depalmitoylation enzymes.
High expression of APT1 (show FAS ELISA Kits) is associated with chronic lymphocytic leukemia.
identifcation APT1 (show FAS ELISA Kits) as one of the thioesterases in the acylation cycle and demonstration that this protein is a cellular target of the inhibitor.
Serum activity of APT1 (show FAS ELISA Kits) may play an important role in determination of the concentration of des (show DES ELISA Kits)-acyl ghrelin (show GHRL ELISA Kits) in circulation, especially under septic inflammation.
Endogenous and overexpressed hAPT1 were mainly localized in the cytosol, while some signals were detected in the plasma membrane, the nuclear membrane and endoplasmic reticulum in HEK293 cells.
Results suggest that APT1 (show FAS ELISA Kits)-regulated depalmitoylation of Galpha (show SUCLG1 ELISA Kits)(13) might be an important downstream event of miR (show MLXIP ELISA Kits)-138 function.
Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. The use of alternate polyadenylation sites has been found for this gene. There are alternatively spliced transcript variants described for this gene but the full length nature is not known yet.
acyl-protein thioesterase 1
, lysoPLA I
, lysophopholipase 1
, lysophospholipase I
, phospholipase 1a
, lysophospholipid-specific lysophospholipase
, lysophospholipase 1
, calcium-independent phospholipase A2