|Application ||WB, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||36 KDa|
|Antigen Region||163-189 aa|
|Other Names||Acyl-coenzyme A thioesterase 8, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, PTE-1, Peroxisomal long-chain acyl-CoA thioesterase 1, Thioesterase II, hACTE-III, hACTEIII, hTE, ACOT8, ACTEIII, PTE1, PTE2|
|Format||Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.|
|Synonyms||ACTEIII, PTE1, PTE2|
|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:9299485, PubMed:9153233, PubMed:15194431). Competes with bile acid CoA:amino acid N-acyltransferase (BAAT) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (C2 to C20) (PubMed:9299485, PubMed:9153233). Inactive towards substrates with more than C20 aliphatic chains (PubMed:9153233). Involved in the metabolic regulation of peroxisome proliferation (PubMed:15194431).|
|Cellular Location||Cytoplasm. Peroxisome matrix. Note=Predominantly localized in the peroxisome (PubMed:10092594, PubMed:15194431)|
|Tissue Location||Detected in a T-cell line (at protein level). Ubiquitous (PubMed:9153233, PubMed:9299485)|
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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. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation.
Watanabe H.,et al.Biochem. Biophys. Res. Commun. 238:234-239(1997).
Liu L.X.,et al.J. Biol. Chem. 272:13779-13785(1997).
Jones J.M.,et al.J. Biol. Chem. 274:9216-9223(1999).
Deloukas P.,et al.Nature 414:865-871(2001).
Ishizuka M.,et al.Exp. Cell Res. 297:127-141(2004).
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