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anti-Human CRAT Antibodies:
anti-Mouse (Murine) CRAT Antibodies:
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Human Polyclonal CRAT Primary Antibody for WB - ABIN4265005
Schönke, Björnholm, Chibalin, Zierath, Deshmukh: Proteomics Analysis of Skeletal Muscle from Leptin-Deficient ob/ob Mice Reveals Adaptive Remodeling of Metabolic Characteristics and Fiber Type Composition. in Proteomics 2019
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Human Polyclonal CRAT Primary Antibody for ELISA, WB - ABIN560457
von Leitner, Klinke, Atzler, Slocum, Lund, Kielstein, Maas, Schmidt-Haupt, Pekarova, Hellwinkel, Tsikas, DAlecy, Lau, Willems, Kubala, Ehmke, Meinertz, Blankenberg, Schwedhelm, Gadegbeku, Böger et al.: Pathogenic cycle between the endogenous nitric oxide synthase inhibitor asymmetrical dimethylarginine and the leukocyte-derived hemoprotein myeloperoxidase. ... in Circulation 2011
We provide evidence that the downregulation of hsa-miR-124-3p, hsa-miR-129-5p and hsa-miR-378 induced an increase in both expression and activity of CPT1A, CACT and CrAT in malignant prostate cells.
CrAT turned out to be active towards some but not all the BCAAO intermediates tested and no activity was found with dicarboxylic acyl-CoA esters.
the purification, crystallization and preliminary X-ray crystallographic studies of human carnitine acetyltransferase are reported
The structure and reactions of this enzyme are examined.
structure of a binary complex of human peroxisomal carnitine acetyltransferase and the substrate l-carnitine, refined to a resolution of 1.8; site-directed mutagenesis and kinetic characterization
Data show that CrAT overexpression in primary human skeletal myocytes increased glucose uptake and attenuated lipid-induced suppression of glucose oxidation.
Human CPT1A, CPT1B, CPT2, CROT and CRAT are known to encode active carnitine acyltransferases. Earlier pfam annotations refer to the non-existing compound CARNITATE. In 2000 this has been changed to CARNITINE.
we modeled mitochondrial overload by creating mice lacking the enzyme carnitine acetyltransferase (CrAT) in the proximal tubules, thus limiting a primary mechanism to export carbons under conditions of substrate excess. Mice developed tubular disease and, interestingly, secondary glomerulosclerosis. This was accompanied by increased levels of apoptosis, fibrosis and oxidative stress.
AgRP neurons require Crat to provide the metabolic flexibility to optimize nutrient partitioning and regulate peripheral substrate utilization, particularly during fasting and refeeding.
Crat within AgRP neurons forms a component of the homeostatic response to restricted feeding but is not likely to be a molecular component of Food-entrainable oscillator.
Presence of a cytosolic CrAT with a low Km for CoA, favoring the formation of cytosolic acetyl-CoA, providing an additional source to the classical ATP-citrate lyase pathway; there is an inverse relation between CrAT and the ratio of acetyl-CoA/CoA as evident in conditions affecting the regulation of cardiac energy metabolism.
Studies revealed that ablation of CrAT in myeloid lineage cells did not impact glucose homeostasis, insulin-action, adipose tissue leukocytosis, and inflammation when animals were confronted with a variety of metabolic stressors, including high-fat diet, fasting, or LPS-induced acute endotoxemia.
Crat-mediated acetyl group buffering is essential for optimal exercise performance.
structural model for L-CPT I (liver CPT I), based on the similarity of this enzyme to the recently crystallized mouse carnitine acetyltransferase
the M564G or M564A mutation is sufficient to increase the activity of the enzyme toward medium-chain substrates
The predicted full length cDNA sequence of the porcine CRAT gene was characterised and a new 5' variant for dog, rat and mouse was proposed.
This gene encodes carnitine acetyltransferase (CRAT), which is a key enzyme in the metabolic pathway in mitochondria, peroxisomes and endoplasmic reticulum. CRAT catalyzes the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine and regulates the ratio of acylCoA/CoA in the subcellular compartments. Two transcript variants encoding different isoforms have been found for this gene.
, carnitine acetylase
, carnitine acetyltransferase
, carnitine O-acetyltransferase
, Carnitine acetyltransferase
, carnitine acetyl transferase
, Carnitine acetylase