ACOT8 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, E |
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Primary Accession | O14734 |
Reactivity | Human, Rat, Mouse |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 35914 Da |
Gene ID | 10005 |
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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 |
Target/Specificity | This ACOT8 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 275-310 amino acids from the C-terminal region of human ACOT8. |
Dilution | WB~~1:2000 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | ACOT8 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ACOT8 |
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Synonyms | ACTEIII, PTE1 {ECO:0000303|PubMed:100925 |
Function | Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:15194431, PubMed:9153233, PubMed:9299485). Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:9153233, PubMed:9299485). 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) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (PubMed:15194431). |
Cellular Location | Peroxisome matrix. Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded |
Tissue Location | Detected in a T-cell line (at protein level). Ubiquitous (PubMed:9153233, PubMed:9299485) |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
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.
REFERENCES
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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