Acot8 (GeneName), Acyl-coenzyme A thioesterase 8 (ProteinName), ACOT8_MOUSE.
Mouse Acot8/ Acyl-coenzyme A thioesterase 8 ELISA Kit
Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, Peroxisomal acyl-CoA thioesterase 2, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, PTE-1, Peroxisomal long-chain acyl-CoA thioesterase 1, Pte1
Natural and recombinant mouse Acyl-coenzyme A thioesterase 8
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:11673457). Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (PubMed:11673457). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:11673457). Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (PubMed:11673457). ACOT8 is also able to hydrolyze CoA esters of dicarboxylic acids (PubMed:16141203). It is involved in the metabolic regulation of peroxisome proliferation (By similarity).
Peroxisome matrix Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded.
MSAPEGLGDA | HGDADRGDLS | GDLRSVLVTS | VLNLEPLDED | LYRGRHYWVP |
TSQRLFGGQI | MGQALVAAA | KSVSEDVHVH | SLHCYFVRAG | DPKVPVLYHV |
ERIRTGASFS | VRAVKAVQHG | K AIFICQAS | FQQMQPSPLQ | HQFSMPSVPP |
PEDLLDHEAL | IDQYLRDPNL | HKKYRVGLNR | VA AQEVPIE | IKVVNPPTLT |
QLQALEPKQM | FWVRARGYIG | EGDIKMHCCV | AAYISDYAFL | GTA LLPHQS |
KYKVNFMASL | DHSMWFHAPF | RADHWMLYEC | ESPWAGGSRG | LVHGRLWRRD |
GVLA VTCAQ | EGVIRLKPQV | SESKL
This product has not yet been referenced specifically in any publications.
"Identification of peroxisomal acyl-CoA thioesterases in yeast and humans."
"Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation."
"A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef."
"Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs."
"A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases."
"The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes."
"Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis."
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
"The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism."
"The DNA sequence and comparative analysis of human chromosome 20."
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