ACOT8, Recombinant, Human, aa1-319, His-Tag (Acyl-coenzyme A Thioesterase 8, ACTEIII, PTE1, PTE2, Acyl-CoA Thioesterase 8, Choloyl-coenzyme A Thioesterase, HIV-Nef-associated acyl-CoA Thioesterase, PTE-2, Peroxisomal Acyl-coenzyme A Thioester Hydrolase 1, Peroxisomal Long-chain Acyl-CoA Thioesterase 1, Thioesterase II)

Acyl-coenzyme A thioesterase 8, also known as ACOT8, 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. This protein may mediate Nef-induced down- regulation of CD4. It competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). ACOT8 shows a preference for medium-length fatty acyl-CoAs.

Source:
Recombinant protein corresponding to human ACOT8, fused to His-tag at N- terminal expressed in E.coli.

Molecular Weight:
~38.3kD (342aa) (MALDI-TOF)

Amino Acid Sequence:
MGSSHHHHHH SSGLVPRGSH MGSMSSPQAP EDGQGCGDRG DPPGDLRSVL VTTVLNLEPL DEDLFRGRHY WVPAKRLFGG QIVGQALVAA AKSVSEDVHV HSLHCYFVRA GDPKLPVLYQ VERTRTGSSF SVRSVKAVQH GKPIFICQAS FQQAQPSPMQ HQFSMPTVPP PEELLDCETL IDQYLRDPNL QKRYPLALNR IAAQEVPIEI KPVNPSPLSQ LQRMEPKQMF WVRARGYIGE GDMKMHCCVA AYISDYAFLG TALLPHQWQH KVHFMVSLDH SMWFHAPFRA DHWMLYECES PWAGGSRGLV HGRLWRQDGV LAVTCAQEGV IRVKPQVSES KL

Enzyme Activity:
Not determined. This product is recommended for use in applications that do not require a catalytically active form of the protein.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.