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WIG1 (show ZMAT3 Proteins) governs the miRNA-dependent and the miRNA-independent recruitment of AGO2 (show EIF2C2 Proteins) to lower the stability of and suppress the translation of ACOT7 mRNA.
the human BACH gene can express long-chain acyl-CoA hydrolase (show ACOT1 Proteins) activity in multiple intracellular compartments by generating BACH isoforms with differential localization signals to affect various cellular functions that involve acyl-CoAs
Data (including data from studies in transgenic mice) suggest that up-regulation of Acot7 expression in clonal beta-cells impairs insulin (show INS Proteins) secretion in response to glucose plus free fatty acids; expression of Acot7 is ubiquitous across tissues but relatively silenced/disallowed in pancreatic beta cells.
ACOT7 may be involved in dietary intake-associated responses in fatty acid metabolism in mesenteric lymph nodes.
ACOT7 counterregulates fatty acid metabolism in neurons and protects against neurotoxicity.
Acot7 gene is expressed as multiple isoforms in a tissue-specific manner; expression in tissues other than brain and testis is likely to play important roles in fatty acid metabolism.
The structural basis for recruitmment of tandem domains in Acot7 is demonstrated and its role in inflammation presented.
This gene encodes a member of the acyl coenzyme family. The encoded protein hydrolyzes the CoA thioester of palmitoyl-CoA and other long-chain fatty acids. Decreased expression of this gene may be associated with mesial temporal lobe epilepsy. Alternatively spliced transcript variants encoding distinct isoforms with different subcellular locations have been characterized.
acyl-CoA thioesterase 7
, cytosolic acyl coenzyme A thioester hydrolase
, cytosolic acyl coenzyme A thioester hydrolase-like
, brain acyl-CoA hydrolase
, acyl-CoA thioesterase 2
, acyl-CoA thioesterase, long chain
, brain acyl CoA hydrolase
, long chain acyl-CoA thioester hydrolase
, 50-kDa brain acyl-CoA hydrolase