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Recombinant Human Acyl-coenzyme A thioesterase 8 (ACOT8)

Recombinant Human Acyl-coenzyme A thioesterase 8 (ACOT8)

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

ACOT8

Uniprot NO.

O14734

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-319

Target Protein Sequence

MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP AKRLFGGQIV GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER TRTGSSFSVR SVKAVQHGKP IFICQASFQQ AQPSPMQHQF SMPTVPPPEE LLDCETLIDQ YLRDPNLQKR YPLALNRIAA QEVPIEIKPV NPSPLSQLQR MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL LPHQWQHKVH FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV TCAQEGVIRV KPQVSESKL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full length protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs. Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. 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). Is also able to hydrolyze CoA esters of dicarboxylic acids. It is involved in the metabolic regulation of peroxisome proliferation.; (Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression.

Gene References into Functions

In summary, lipolytic enzyme ACOT8 is frequently upregulated in HCC clinical specimens. More importantly, ACOT8 silencing leads to inhibition of cell growth in HCC in vitro. PMID:24788990
Acyl-CoA thioesterase 8 is a specific protein related to nodal metastasis and prognosis of lung adenocarcinoma. PMID:23540296
ACOT4 and ACOT8 are responsible for the termination of beta-oxidation of dicarboxylic acids of medium-chain length with the concomitant release of the corresponding free acids PMID:16141203
SREBP2 modulates brain palmitoyl-coa hydrolase gene transcription. PMID:16335799
An isoform of long-chain acyl-CoA hydrolase may be responsible for the nafamostat hydrolysis in human liver cytosol. PMID:17624024