ACADS Antibody (G-10): sc-365953

ACADS Antibody (G-10) is a mouse monoclonal IgG2b kappa light chain antibody that detects ACADS protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). ACADS (G-10) antibody is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. ACADS protein, also known as acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain, or SCAD, is a crucial 412 amino acid homotetrameric mitochondrial flavoprotein that plays a vital role in the mitochondrial fatty acid beta-oxidation pathway by catalyzing the rate-limiting step. This function is essential for proper metabolism of fatty acids, and deficiencies in ACADS can lead to serious metabolic disorders, including short-chain acyl-CoA dehydrogenase deficiency, which manifests as acute acidosis and muscle weakness in infants, as well as lipid-storage myopathy in adults. The accumulation of butyrylcarnitine and ethylmalonic acid in blood and urine due to ACADS mutations highlights the importance of ACADS in maintaining metabolic homeostasis. Additionally, ACADS contains four flavin adenine dinucleotide (FAD) domains, which are critical for enzymatic activity and stability, further underscoring the significance of ACADS in cellular metabolism.

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ACADS Antibody (G-10) References:

1. Deficiency in short-chain fatty acid beta-oxidation affects theta oscillations during sleep.  |  Tafti, M., et al. 2003. Nat Genet. 34: 320-5. PMID: 12796782
2. Thermal unfolding of medium-chain acyl-CoA dehydrogenase and iso(3)valeryl-CoA dehydrogenase: study of the effect of genetic defects on enzyme stability.  |  Nasser, I., et al. 2004. Biochim Biophys Acta. 1690: 22-32. PMID: 15337167
3. Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids.  |  Ensenauer, R., et al. 2005. J Biol Chem. 280: 32309-16. PMID: 16020546
4. Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover.  |  Nagpal, A., et al. 2006. Biochemistry. 45: 1138-50. PMID: 16430210
5. Clinical, biochemical, and genetic heterogeneity in short-chain acyl-coenzyme A dehydrogenase deficiency.  |  van Maldegem, BT., et al. 2006. JAMA. 296: 943-52. PMID: 16926354
6. Short-chain acyl-CoA dehydrogenase gene mutation (c.319C>T) presents with clinical heterogeneity and is candidate founder mutation in individuals of Ashkenazi Jewish origin.  |  Tein, I., et al. 2008. Mol Genet Metab. 93: 179-89. PMID: 18054510
7. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase.  |  McAndrew, RP., et al. 2008. J Biol Chem. 283: 9435-43. PMID: 18227065
8. The regulation of acyl-CoA dehydrogenases in adipose tissue by rosiglitazone.  |  Goetzman, ES. 2009. Obesity (Silver Spring). 17: 196-8. PMID: 18948967
9. Compound heterozygous mutations of ACADS gene in newborn with short chain acyl-CoA dehydrogenase deficiency: case report and literatures review.  |  An, SJ., et al. 2016. Korean J Pediatr. 59: S45-S48. PMID: 28018444
10. An unusually high frequency of SCAD deficiency caused by two pathogenic variants in the ACADS gene and its relationship to the ethnic structure in Slovakia.  |  Lisyová, J., et al. 2018. BMC Med Genet. 19: 64. PMID: 29678161
11. ACAD10 and ACAD11 enable mammalian 4-hydroxy acid lipid catabolism.  |  Rashan, EH., et al. 2024. bioRxiv.. PMID: 38260250
12. Structural organization of the human short-chain acyl-CoA dehydrogenase gene.  |  Corydon, MJ., et al. 1997. Mamm Genome. 8: 922-6. PMID: 9383286

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-ACADS Antibody (G-10) has 6 citations in a variety of scientific publications.

Primary antibodies like Anti-ACADS Antibody (G-10) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

ACADS Antibody (G-10) Specifications

Alternate Product Name: ACADS

Product Clone Name: G-10

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG_2b kappa light chain

Amino Acids: 104-244

Epitope Target: ACADS

Epitope Species: human

Product Reactivity/Detection: ACADS

Species Reactivity/Detection: mouse, rat, human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, IHC(P), ELISA

Vialing Information: Each vial contains 200 µg IgG_2b kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 6 citations in various scientific publications

Available Conjugates/Forms for ACADS Antibody (G-10): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin