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Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. Zusätzlich bieten wir Ihnen Lysophospholipase I Antikörper (65) und Lysophospholipase I Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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Data indicate that thioesterases APT1 (zeige FAS Proteine)/APT2 (zeige TAP2 Proteine) depalmitoylate nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2 (zeige NMNAT2 Proteine)) and zDHHC17 (zeige ZDHHC17 Proteine) is the strongest candidate palmitoyltransferase for NMNAT2 (zeige NMNAT2 Proteine).
Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 (zeige LYPLA2 Proteine) with that of proto-oncogene (zeige RAB1A Proteine) H-ras (zeige HRAS Proteine) product and growth-associated protein-43 (zeige GAP43 Proteine)
Here, we describe the conserved functions of APT1 (zeige FAS Proteine) and APT2 (zeige TAP2 Proteine) across organisms and discuss the possibility that these enzymes are members of a larger family of depalmitoylation enzymes.
High expression of APT1 (zeige FAS Proteine) is associated with chronic lymphocytic leukemia.
identifcation APT1 (zeige FAS Proteine) 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 (zeige FAS Proteine) may play an important role in determination of the concentration of des (zeige DES Proteine)-acyl ghrelin (zeige GHRL Proteine) 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 (zeige FAS Proteine)-regulated depalmitoylation of Galpha (zeige SUCLG1 Proteine)(13) might be an important downstream event of miR (zeige MLXIP Proteine)-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