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anti-Human ACADSB Antikörper:
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These findings confirm that SBCAD deficiency can be identified through newborn screening by acylcarnitine analysis.
Identification and characterization of an IVS3+3A>G mutation (c.303+3A>G) in the SBCAD gene, and provide evidence that this mutation is disease-causing.
Results examine the mechanistic basis for dysfunction of the common variant short-chain acyl-CoA (zeige GNPAT Antikörper) dehydrogenases and demonstrate that mutations can have a large impact on the redox properties of the enzyme.
Results indicate that substrate redox activation occurs in short-chain acyl-CoA dehydrogenase (zeige Acads Antikörper) leading to a large enzyme midpoint potential shift.
Short/branched chain acyl-CoA dehydrogenase(ACADSB) is a member of the acyl-CoA dehydrogenase family of enzymes that catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branch chained amino acids. Substrate specificity is the primary characteristic used to define members of this gene family. The ACADSB gene product has the greatest activity towards the short branched chain acyl-CoA derivative, (S)-2-methylbutyryl-CoA, but also reacts significantly with other 2-methyl branched chain substrates and with short straight chain acyl-CoAs. The cDNA encodes for a mitochondrial precursor protein which is cleaved upon mitochondrial import and predicted to yield a mature peptide of approximately 43.7-KDa.
acyl-Coenzyme A dehydrogenase, short/branched chain
, short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
, acyl-coenzyme A dehydrogenase, short/branched chain
, 2-methyl branched chain acyl-CoA dehydrogenase
, 2-methylbutyryl-coenzyme A dehydrogenase
, 2-methylbutyryl-CoA dehydrogenase
, Acyl-Coenzyme A dehydrogenase short-branched chain