The image on the left is immunohistochemistry of paraffin-embedded Human colon cancer tissue using CSB-PA957686(ACADS Antibody) at dilution 1/20, on the right is treated with fusion protein. (Original magnification: ×200)
The image on the left is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using CSB-PA957686(ACADS Antibody) at dilution 1/20, on the right is treated with fusion protein. (Original magnification: ×200)
Gel: 10%SDS-PAGE, Lysate: 40 μg, Lane 1-3: Human liver cancer tissue, rat kidney tissue, human fetal liver tissue, Primary antibody: CSB-PA957686(ACADS Antibody) at dilution 1/400, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 90 seconds
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貨期:
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains.
基因功能參考文獻:
a link between ACADS susceptibility variants and abnormal beta-oxidation consistent with known altered kinetics of these variants PMID: 28532786
Korean patients with Short-chain acyl-CoA dehydrogenase deficiency showed heterogenous clinical features and ACADS genotype. PMID: 27466294
Thirteen proteins had significant alteration in protein levels in patients carrying variation c.319C>T in ACADS compared to controls and they belonged to various pathways, such as the antioxidant system and amino acid metabolism. PMID: 24485985
Results show significant upregulation of LASP1 and SCAD protein levels in acute psychotic bipolar disorder samples. PMID: 24554194
IVD mutations in Asian populations are distinct from these in Western populations. PMID: 22004070
physiological concentrations of flavin adenine dinucleotide resulted in a spectacular enhancement of the thermal stabilities of SCAD and prevented enzymatic activity loss PMID: 21968293
In glucose-tolerant individuals the minor C-allele of rs2014355 of ACADS was associated with reduced measures of glucose-stimulated insulin release during an oral glucose tolerance test. PMID: 21211036
We therefore propose that SCAD misfolding leads to production of ROS, which in turn leads to fission and a grain-like structure of the mitochondrial reticulum. This finding indicates a toxic response elicited by misfolded p.Arg83Cys SCAD proteins PMID: 20371198
Molecular pathogenesis of a novel mutation, G108D, in ACADS identified in subjects with ACADS deficiency. PMID: 20376488
Reduction of catalytic activity and stability in polymorphic variant of SCAD (Gly185Ser) is caused by decreased flexibility in the tertiary conformation of the mutant enzyme. PMID: 12220177
Replacement of the catalytic glutamate in either short-chain acyl-CoA dehydrogenase (SCAD) or isovaleryl-CoA dehydrogenase (IVD)with glycine resulted in a several-fold reduction in affinity for substrate. PMID: 16376132
One of 220 SIDs cases was homozygous for the prevalent MCAD A985G mutation. PMID: 18045290
The c.319C>T mutation can lead to wide clinical and biochemical phenotypic variability, suggesting a complex multifactorial/polygenic condition. This should be screened for in individuals with multicore myopathy, particularly among the Ashkenazim. PMID: 18054510
A homozygous variant allele of the SCAD gene, 625G>A, was detected in new case of short-chain acyl-CoA dehydrogenase deficiency. PMID: 18175080
Extensive laboratory investigations indicate that the short-chain acyl-CoA dehydrogenase gene variant is likely preventing or delaying the normal expression of the Prader-Willi syndrome phenotype. PMID: 18184946
SCAD deficiency should be considered as a disorder of protein folding that can lead to clinical disease in combination with other genetic and environmental factors. PMID: 18523805
A deoxyribonucleic analysis revealed the presence of a 625G>A (G-to-A substitution at nucleotide 625) variant short-chain acyl-coenzyme A dehydrogenase gene polymorphism. PMID: 18539996
SCAD deficiency cause a disorder that leads to the accumulation of butyrylcarnitine and ethylmalonic acid in blood and urine. PMID: 18977676