Product Name: ACADM Antibody
Species Reactivity: Human
Tested Applications: ELISA, WB
Applications: ACADM antibody can be used for detection of ACADM by ELISA at 1:1562500. ACADM antibody can be used for detection of ACADM by western blot at 1 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 – 100,000.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 46 kDa
Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human ACADM.
Host Species: Rabbit
Purification: Antibody is purified by peptide affinity chromatography method.
Physical State: Lyophilized
CAS NO.: 30964-13-7
Product: Cynarin
Buffer: Antibody is lyophilized in PBS buffer with 2% sucrose. Add 50 μL of distilled water. Final antibody concentration is 1 mg/mL.
Concentration: 1 mg/ml
Storage Conditions: For short periods of storage (days) store at 4˚C. For longer periods of storage, store ACADM antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: ACADM, ACAD1, MCAD, MCADH
Accession NO.: NP_000007
Protein Ino: 4557231
Official Symbol: ACADM
Geneid: 34
Background: ACADM Is the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Clinical phenotypes are associated with ACADM hereditary deficiency.This gene encodes the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Defects in this gene cause medium-chain acyl-CoA dehydrogenase deficiency, a disease characterized by hepatic dysfunction, fasting hypoglycemia, and encephalopathy, which can result in infantile death. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
PubMed ID:http://aac.asm.org/content/52/1/248.abstract
