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anti-Mouse (Murine) CRAT Antibodies:
anti-Human CRAT Antibodies:
anti-Rat (Rattus) CRAT Antibodies:
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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
Crat-mediated acetyl group buffering is essential for optimal exercise performance.
structural model for L-CPT I (show CPT1A Antibodies) (liver CPT I (show CPT1A Antibodies)), based on the similarity of this enzyme to the recently crystallized mouse carnitine acetyltransferase
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.
We provide evidence that the downregulation of hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-124-3p, hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-129-5p and hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-378 induced an increase in both expression and activity of CPT1A (show CPT1A Antibodies), CACT (show SLC25A20 Antibodies) 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 (show GNPAT Antibodies) esters.
the purification, crystallization and preliminary X-ray crystallographic studies of human carnitine acetyltransferase are reported
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 (show CPT1A Antibodies), CPT1B (show CPT1B Antibodies), CPT2 (show CPT2 Antibodies), CROT (show CROT Antibodies) 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.
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 acetyltransferase
, carnitine O-acetyltransferase
, carnitine acetylase
, carnitine acetyl transferase