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C4899

Sigma-Aldrich

Carnitine Acetyltransferase from pigeon breast muscle

ammonium sulfate suspension, ≥50 units/mg protein

Synonyme(s) :

CrAT

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

pigeon breast

Forme

ammonium sulfate suspension

Activité spécifique

≥50 units/mg protein

Concentration

≥0.4 mg/mL

Technique(s)

cell based assay: suitable

Numéro d'accès Protein ID

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

pigeon ... CRAT(102084317)

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Description générale

Research area: Cell Signaling

Application

Carnitine Acetyltransferase from pigeon breast muscle has been used in enzymatic assays.

Actions biochimiques/physiologiques

Carnitine acyltransferases (CrAT) are enzymes that contribute to the reversible conversion of acetyl-CoA and carnitine into acetylcarnitine and free CoA. This enzymatic process plays a vital role in the energy metabolism of eukaryotes by promoting the β-oxidation of fatty acids. CrAT-mediated acetyl carnitine production and efflux help maintain a balance between acetyl-CoA and acetyl carnitine in the mitochondria, regenerate free CoA, and alleviate the product inhibition of pyruvate dehydrogenase (PDH), which is a key enzyme in glucose oxidation. This process promotes glucose homeostasis and helps maintain optimal cellular energy metabolism. Carnitine acetyltransferase activity also aids in the progression of the cell cycle from G1 to S phase. carnitine acetyltransferase deficiency also leads to the development of various neurological disorders including Alzheimer′s disease, ataxic encephalopathy, and several vascular diseases.
Carnitine acetyltransferase maintains the cellular and mitochondrial levels of acetyl-CoA, a key cofactor required for oxidative metabolism, by catalyzing an equilibrium between acetyl-CoA and acetyl-L-carnitine, a storage form of activated acetate. Carnitine acetyltransferase also maintains the pool of acetyl-CoA required for neuronal and nonneuronal acetylcholine production.

Définition de l'unité

One unit will convert 1.0 μmole of acetyl-L-carnitine and CoA to L-carnitine and acetyl-CoA per min at pH 8.0 at 25 °C.

Forme physique

Crystalline suspension in 3.2 M (NH4)2SO4 solution, 50 mM potassium phosphate, 1 mM dithiothreitol, pH 7.0

Remarque sur l'analyse

Protein determined by biuret.

Inhibiteur

Réf. du produit
Description
Tarif

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Redesign of carnitine acetyltransferase specificity by protein engineering
Cordente AG, et al.
The Journal of Biological Chemistry, 279(32), 33899-33908 (2004)
Structure-based virtual screening to identify novel carnitine acetyltransferase activators
Ombrato R, et al.
Journal of Molecular Graphics & Modelling (2020)
Ann T Hanna-Mitchell et al.
Life sciences, 80(24-25), 2298-2302 (2007-03-17)
Non-neuronal release of acetylcholine (ACh) has been proposed to play a role in urinary bladder function. These studies investigated the expression and function of the non-neuronal cholinergic system in cultured urothelial cells isolated from the rat urinary bladder. Our findings
Marie A Schroeder et al.
Circulation. Cardiovascular imaging, 5(2), 201-209 (2012-01-13)
Carnitine acetyltransferase catalyzes the reversible conversion of acetyl-coenzyme A (CoA) into acetylcarnitine. The aim of this study was to use the metabolic tracer hyperpolarized [2-(13)C]pyruvate with magnetic resonance spectroscopy to determine whether carnitine acetyltransferase facilitates carbohydrate oxidation in the heart.
Rui Wu et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(9), 3259-3263 (2012-02-14)
Phenotypic plasticity occurs prevalently and plays a vital role in adaptive evolution. However, the underlying molecular mechanisms responsible for the expression of alternate phenotypes remain unknown. Here, a density-dependent phase polyphenism of Locusta migratoria was used as the study model

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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