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Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. De plus, nous expédions Lysophospholipase I Anticorps (65) et Lysophospholipase I Protéines (19) et beaucoup plus de produits pour cette protéine.
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Data show taht active S-depalmitoylation in mitochondria, in part mediated by acyl-protein thioesterase 1 (APT1)
Here, we describe the conserved functions of APT1 and APT2 across organisms and discuss the possibility that these enzymes are members of a larger family of depalmitoylation enzymes.
High expression of APT1 (Montrer FAS Kits ELISA) is associated with chronic lymphocytic leukemia.
identifcation APT1 (Montrer FAS Kits ELISA) as one of the thioesterases in the acylation cycle and demonstration that this protein is a cellular target of the inhibitor.
Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with that of proto-oncogene (Montrer RAB1A Kits ELISA) H-ras (Montrer HRAS Kits ELISA) product and growth-associated protein-43 (Montrer GAP43 Kits ELISA)
Serum activity of APT1 (Montrer FAS Kits ELISA) may play an important role in determination of the concentration of des (Montrer DES Kits ELISA)-acyl ghrelin (Montrer GHRL Kits ELISA) 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 (Montrer FAS Kits ELISA)-regulated depalmitoylation of Galpha(13) might be an important downstream event of miR (Montrer MLXIP Kits ELISA)-138 function.
Data indicate that thioesterases APT1/APT2 depalmitoylate nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) and zDHHC17 is the strongest candidate palmitoyltransferase for NMNAT2.
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
, lysophospholipid-specific lysophospholipase
, lysophopholipase 1
, lysophospholipase I
, phospholipase 1a
, lysophospholipase 1
, calcium-independent phospholipase A2