ACOT8 (GeneName), Acyl-coenzyme A thioesterase 8 (ProteinName), ACOT8_HUMAN.
Human ACOT8/ Acyl-coenzyme A thioesterase 8 ELISA Kit
Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, Peroxisomal acyl-coenzyme A thioester hydrolase 1, PTE-1, Peroxisomal long-chain acyl-CoA thioesterase 1, Thioesterase II, hACTE-III, ACTEIII, PTE1, Peroxisomal acyl-CoA thioesterase 2, PTE-2
Natural and recombinant human Acyl-coenzyme A thioesterase 8
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
(Microbial infection) Interacts with human immunodeficiency virus (HIV-1) Nef (via middle region); this interaction enhances ACOT8 Acyl-CoA thioesterase activity and occurs in a Nef myristoylation-independent manner (PubMed:9299485). According to a second report, the interaction with HIV-1 Nef occurs in a Nef myristoylation-independent manner but does not enhance ACOT8 Acyl-CoA thioesterase activity (PubMed:9153233).
(Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression (PubMed:9153233).
Peroxisome matrix Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded.
MSSPQAPEDG | QGCGDRGDPP | GDLRSVLVTT | VLNLEPLDED | LFRGRHYWVP |
AKRLFGGQIV | GQALVAAAK | SVSEDVHVHS | LHCYFVRAGD | PKLPVLYQVE |
RTRTGSSFSV | RSVKAVQHGK | P IFICQASF | QQAQPSPMQH | QFSMPTVPPP |
EELLDCETLI | DQYLRDPNLQ | KRYPLALNRI | AA QEVPIEI | KPVNPSPLSQ |
LQRMEPKQMF | WVRARGYIGE | GDMKMHCCVA | AYISDYAFLG | TAL LPHQWQ |
HKVHFMVSLD | HSMWFHAPFR | ADHWMLYECE | SPWAGGSRGL | VHGRLWRQDG |
VLAV TCAQE | GVIRVKPQVS | ESKL
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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