Anti-ACAT1 Antibody Picoband® fluoro488 Vervoeging

Acetyl-CoA acetyltransferase, mitochondrial, also known as acetoacetyl-CoA thiolase, is an enzyme that in humans is encoded by the ACAT1 (Acetyl-Coenzyme A acetyltransferase 1) gene. This gene encodes a mitochondrially localized enzyme that catalyzes the reversible formation of acetoacetyl-CoA from two molecules of acetyl-CoA. Defects in this gene are associated with 3-ketothiolase deficiency, an inborn error of isoleucine catabolism characterized by urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, tiglylglycine, and butanone.

Bifunctional epoxide hydrolase 2; Cytosolic epoxide hydrolase 2; CEH;3.3.2.10; Epoxide hydratase; Soluble epoxide hydrolase; SEH; Lipid-phosphate phosphatase;3.1.3.76; EPHX2

ACAT1

38

P24752

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human ACAT1 recombinant protein (Position: S10-Q404) .

Ubiquitous. A high level expression is seen in secretory tissues.

Flow Cytometry

Cancer Metabolism, Cardiovascular, Cell Biology, Cholesterol Metabolism, Drug Metabolism, Fatty Acid Oxidation, Fatty Acids, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Redox Metabolism, Signal Transduction, Vasculature

Immunogen affinity purified.

Liquid

Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo- 9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro- 9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy- octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate. .

1. Daum, R. S., Scriver, C. R., Mamer, O. A., Delvin, E., Lamm, P. H., Goldman, H. An inherited disorder of isoleucine catabolism causing accumulation of alpha-methylacetoacetate and alpha-methyl-beta-hydroxybutyrate and intermittent metabolic acidosis. Pediat. Res. 7: 149-160, 1973. 2. Fukao, T., Matsuo, N., Zhang, G. X., Urasawa, R., Kubo, T., Kohno, Y., Kondo, N. Single base substitutions at the initiator codon in the mitochondrial acetoacetyl-CoA thiolase (ACAT1/T2) gene result in production of varying amounts of wild-type T2 polypeptide. Hum. Mutat. 21: 587-592, 2003. 3. Fukao, T., Nakamura, H., Nakamura, K., Perez-Cerda, C., Baldellou, A., Barrionuevo, C. R., Castello, F. G., Kohno, Y., Ugarte, M., Kondo, N. Characterization of six mutations in five Spanish patients with mitochondrial acetoacetyl-CoA thiolase deficiency: effects of amino acid substitutions on tertiary structure. Molec. Genet. Metab. 75: 235-243, 2002.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

62616 MW

6

Bifunctional epoxide hydrolase 2

Cytoplasm. Peroxisome.

Bifunctional epoxide hydrolase 2

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.