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Acot8 (GeneName), Acyl-coenzyme A thioesterase 8 (ProteinName), ACOT8_MOUSE.
Product Name:

Mouse Acot8/ Acyl-coenzyme A thioesterase 8 ELISA Kit

Cat.#:
-
Brand:
EIAab®
Regulatory Status:
Alternative:

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

Detection Method:
ELISA
Specificity:
Natural and recombinant mouse Acyl-coenzyme A thioesterase 8
Sample Type:
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Sample Data:
Research Area:
Cardiovascular
Mouse Acot8 ELISA Kit
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Product Datasheets


General Annotation


Sub Unit:
homodimer.


Function:
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).


Subcellular Location:
Peroxisome matrix Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded.


This product has not yet been referenced specifically in any publications.

[1].
"Identification of peroxisomal acyl-CoA thioesterases in yeast and humans."

[2].
"Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation."

[3].
"A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef."

[4].
"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."

[5].
"A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases."

[6].
"The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes."

[7].
"Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis."

[8].
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."

[9].
"The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism."

[10].
"The DNA sequence and comparative analysis of human chromosome 20."
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