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The protein encoded by ABHD5 belongs to a large family of proteins defined by an alpha/beta hydrolase fold, and contains three sequence motifs that correspond to a catalytic triad found in the esterase/lipase/thioesterase subfamily. Additionally we are shipping ABHD5 Antibodies (79) and ABHD5 Proteins (9) and many more products for this protein.
Showing 6 out of 7 products:
Prebinding CGI-58 with PI(3 (show PI3 ELISA Kits))P or PI(5 (show SERPINB5 ELISA Kits))P did not alter its coactivation of ATGL (show PNPLA2 ELISA Kits) in vitro. In summary, purified recombinant CGI-58 that is functional as an ATGL (show PNPLA2 ELISA Kits) coactivator lacks LPAAT activity.
It is clear that CGI-58 can regulate TAG hydrolysis by activating the major TAG hydrolase adipose triglyceride lipase (ATGL (show PNPLA2 ELISA Kits)), yet CGI-58 can also regulate lipid metabolism via mechanisms that do not involve ATGL (show PNPLA2 ELISA Kits).
ABHD5 possesses a PNPLA2 (show PNPLA2 ELISA Kits)-independent function in regulating autophagy and tumorigenesis.
These results indicate that HCV taps into the lipid droplet triglyceride reservoir usurping ABHD5 lipase (show LIPG ELISA Kits) cofactor function
Case Report: novel ABHD5 mutation, c.838C > T (p.Arg280*), in trans with p.Arg234* in a Chinese patient with very mild Dorfman-Chanarin syndrome.
Authors show that rat ATGL (show PNPLA2 ELISA Kits), coactivated by rat CGI-58, efficiently hydrolyzes triglycerides and retinyl ester.
novel ABHD5 truncating variant in a twenty nine month old female child, who presented with icthyosiform erythroderma.
simultaneous tryptophan alanine permutations in both arms abolish localization and activity of CGI-58 as opposed to tryptophan substitutions that occur in only one arm.
this study presents clinical and molecular data of four affected relatives with Chanarin-Dorfman syndrome homozygous for a N209X mutation in ABHD5, and provides a short review by comparing patients with N209X homozygous mutations to patients with other ABHD5 mutations.
PLIN5 (show PLIN5 ELISA Kits) was significantly colocated with ATGL (show PNPLA2 ELISA Kits), mitochondria and CGI-58, indicating a close association between the key lipolytic effectors in resting skeletal muscle.
Prebinding CGI-58 with PI(3 (show PI3 ELISA Kits))P or PI(5)P did not alter its coactivation of ATGL (show PNPLA2 ELISA Kits) in vitro. In summary, purified recombinant CGI-58 that is functional as an ATGL (show PNPLA2 ELISA Kits) coactivator lacks LPAAT (show AGPAT1 ELISA Kits) activity.
CGI-58 regulates hepatic neutral lipid storage and inflammation in the genetic absence of ATGL (show PNPLA2 ELISA Kits).
omega-O-AcylCer and CLE formation critically depend on CGI-58 expression in differentiated keratinocytes.
These results demonstrate that macrophage CGI-58 enhances PPAR-gamma (show PPARG ELISA Kits) signaling and thus suppresses inflammatory responsiveness and mitochondrial dysfunction in macrophages.
Here, we identify synthetic ligands that release ABHD5 from PLIN1 (show PLIN1 ELISA Kits) or PLIN5 (show PLIN5 ELISA Kits) without PKA activation and rapidly activate adipocyte and muscle lipolysis.
we identify adipocyte-type fatty acid-binding protein (A-Fabp (show FABP4 ELISA Kits)) and other members of the fatty acid-binding protein (Fabp (show FABP ELISA Kits)) family as interaction partners of Cgi-58.
Data (including data from studies in atherosclerotic knockout mice) suggest CGI58-deficient macrophages store-up triglyceride-rich droplets and have reduced phagocytic capacity, comparable to Atgl- (adipose triglyceride lipase (show PNPLA2 ELISA Kits)-)deficient macrophages.
-mediated phosphorylation of CGI-58 is required for dispersion of CGI-58 from perilipin (show PLIN1 ELISA Kits) 1A-coated lipid droplets
Muscle CGI-58 deficiency causes cardiac dysfunction and fat deposition in oxidative muscles but induces a series of favorable metabolic changes in mice fed a high-fat diet.
These findings suggest that CGI-58 may be a new target for enhancing the quality of pork products as well as offering the potential of CGI-58 for human obesity treatment.
The protein encoded by this gene belongs to a large family of proteins defined by an alpha/beta hydrolase fold, and contains three sequence motifs that correspond to a catalytic triad found in the esterase/lipase/thioesterase subfamily. It differs from other members of this subfamily in that its putative catalytic triad contains an asparagine instead of the serine residue. Mutations in this gene have been associated with Chanarin-Dorfman syndrome, a triglyceride storage disease with impaired long-chain fatty acid oxidation.
abhydrolase domain containing 5
, CGI58 protein
, 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
, abhydrolase domain-containing protein 5
, lipid droplet-binding protein CGI-58
, alpha/beta hydrolase domain-containing 5
, lipid droplet binding protein
, Abhydrolase domain-containing protein 5