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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 Proteins (9) and ABHD5 Kits (7) and many more products for this protein.
Showing 10 out of 79 products:
Human Polyclonal ABHD5 Primary Antibody for SimWes, WB - ABIN258372
Yamaguchi, Omatsu, Matsushita, Osumi: CGI-58 interacts with perilipin and is localized to lipid droplets. Possible involvement of CGI-58 mislocalization in Chanarin-Dorfman syndrome. in The Journal of biological chemistry 2004
Show all 22 Pubmed References
Human Monoclonal ABHD5 Primary Antibody for IHC (p), ELISA - ABIN565526
Kinney, Qiao, Levaugh, Shao: B56alpha/protein phosphatase 2A inhibits adipose lipolysis in high-fat diet-induced obese mice. in Endocrinology 2010
Show all 11 Pubmed References
Human Monoclonal ABHD5 Primary Antibody for ELISA, WB - ABIN565527
Watt, van Denderen, Castelli, Bruce, Hoy, Kraegen, Macaulay, Kemp: Adipose triglyceride lipase regulation of skeletal muscle lipid metabolism and insulin responsiveness. in Molecular endocrinology (Baltimore, Md.) 2008
Show all 3 Pubmed References
Polyclonal ABHD5 Primary Antibody for WB - ABIN540799
Subramanian, Rothenberg, Gomez, Cohen, Garcia, Bhattacharyya, Shapiro, Dolios, Wang, Lisanti, Brasaemle: Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes. in The Journal of biological chemistry 2004
Show all 3 Pubmed References
Cow (Bovine) Polyclonal ABHD5 Primary Antibody for ICC, IF - ABIN252915
Sitnick, Basantani, Cai, Schoiswohl, Yazbeck, Distefano, Ritov, DeLany, Schreiber, Stolz, Gardner, Kienesberger, Pulinilkunnil, Zechner, Goodpaster, Coen, Kershaw: Skeletal muscle triacylglycerol hydrolysis does not influence metabolic complications of obesity. in Diabetes 2013
Show all 2 Pubmed References
Human Polyclonal ABHD5 Primary Antibody for ELISA, WB - ABIN190850
Lass, Zimmermann, Haemmerle, Riederer, Schoiswohl, Schweiger, Kienesberger, Strauss, Gorkiewicz, Zechner: Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome. in Cell metabolism 2006
Show all 2 Pubmed References
our findings indicate that inhibition of both DGAT1 (show DGAT1 Antibodies) and ABHD5 using siRNA leads to reduction in prostate cancer cell growth.
Prebinding CGI-58 with PI(3 (show PI3 Antibodies))P or PI(5 (show SERPINB5 Antibodies))P did not alter its coactivation of ATGL (show PNPLA2 Antibodies) in vitro. In summary, purified recombinant CGI-58 that is functional as an ATGL (show PNPLA2 Antibodies) coactivator lacks LPAAT (show MBOAT2 Antibodies) activity.
It is clear that CGI-58 can regulate TAG hydrolysis by activating the major TAG hydrolase adipose triglyceride lipase (ATGL (show PNPLA2 Antibodies)), yet CGI-58 can also regulate lipid metabolism via mechanisms that do not involve ATGL (show PNPLA2 Antibodies).
ABHD5 possesses a PNPLA2 (show PNPLA2 Antibodies)-independent function in regulating autophagy and tumorigenesis.
These results indicate that HCV taps (show ASPRV1 Antibodies) into the lipid droplet triglyceride reservoir usurping ABHD5 lipase (show LIPG Antibodies) 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 Antibodies), 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.
Prebinding CGI-58 with PI(3 (show PI3 Antibodies))P or PI(5)P did not alter its coactivation of ATGL (show PNPLA2 Antibodies) in vitro. In summary, purified recombinant CGI-58 that is functional as an ATGL (show PNPLA2 Antibodies) coactivator lacks LPAAT (show AGPAT1 Antibodies) activity.
CGI-58 regulates hepatic neutral lipid storage and inflammation in the genetic absence of ATGL (show PNPLA2 Antibodies).
omega-O-AcylCer and CLE (show C14orf166 Antibodies) formation critically depend on CGI-58 expression in differentiated keratinocytes.
These results demonstrate that macrophage CGI-58 enhances PPAR-gamma (show PPARG Antibodies) signaling and thus suppresses inflammatory responsiveness and mitochondrial dysfunction in macrophages.
Here, we identify synthetic ligands that release ABHD5 from PLIN1 (show PLIN1 Antibodies) or PLIN5 (show PLIN5 Antibodies) without PKA activation and rapidly activate adipocyte and muscle lipolysis.
we identify adipocyte-type fatty acid-binding protein (A-Fabp (show FABP4 Antibodies)) and other members of the fatty acid-binding protein (Fabp (show FABP Antibodies)) 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 Antibodies)-)deficient macrophages.
-mediated phosphorylation of CGI-58 is required for dispersion of CGI-58 from perilipin (show PLIN1 Antibodies) 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