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Product Name: HADHB Polyclonal Antibody, ALEXA FLUOR® 350 Conjugated
Applications: IF(IHC-P)
Reactivity: Human, Mouse, Rat
Conjugation: ALEXA FLUOR® 350
Host: Rabbit
Sourcr: KLH conjugated synthetic peptide derived from human HADHB
Clonality: Polyclonal
CAS NO: 845614-12-2
Product: Naratriptan (hydrochloride)
Isotype: IgG
Concentration: 1ug/ul
Purification: Purified by Protein A.
Storage: Aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Store at 4°C for 12 months.
Synonyms: 2 enoyl Coenzyme A CoA hydratase beta subunit; 3 ketoacyl Coenzyme A CoA thiolase of mitochondrial trunctional protein beta subunit; 3 ketoacyl Coenzyme A thiolase; 3 ketoacyl Coenzyme A thiolase of mitochondrial trunctional protein beta subunit; Acetyl CoA acyltransferase; Beta ketothiolase; ECHB; HADH; Hydroxyacyl Coenzyme A CoA dehydrogenase beta subunit; Hydroxyacyl Coenzyme A dehydrogenase; Hydroxyacyl Coenzyme A dehydrogenase beta subunit; Hydroxyacyl Coenzyme A dehydrogenase/3 ketoacyl Coenzyme A thiolase/enoyl Coenzyme A hydratase trunctional protein beta subunit; Mitochondrial trunctional enzyme beta subunit; Mitochondrial trunctional protein beta subunit; MTPB; TP beta. TPbeta; Trunctional enzyme subunit beta; Trunctional enzyme subunit beta mitochondrial; Trunctional protein; ECHB_HUMAN.
Background: The HADHB gene encodes the beta subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta-oxidation of long chain fatty acids. The mitochondrial membrane-bound heterocomplex is composed of four alpha and four beta subunits, with the beta subunit catalyzing the 3-ketoacyl-CoA thiolase activity. Mutations in this gene result in trifunctional protein deficiency. The encoded protein can also bind RNA and decreases the stability of some mRNAs. The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation. Alternatively spliced transcript variants have been found; however, their full-length nature is not known.
PubMed ID:http://www.ncbi.nlm.nih.gov/pubmed/19439605?dopt=Abstract

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Author: HMTase- hmtase