OXCT1, Polyclonal Antibody

Succinyl-CoA:3-ketoacid coenzyme A transferase 1; mitochondrial; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; OXCT1; OXCT; SCOT

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit Ig

Rabbit

This OXCT1 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 272-306 amino acids from the Central region of human OXCT1.

Purified Rabbit Polyclonal Antibody (Pab)

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Vial Concentration: 0.3 (lot specific)

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-OXCT1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.

Crown Antibodies; Cancer; Metabolism; Signal Transduction

Western Blot (WB), ELISA (EIA)

WB~~1:2000

All lanes : Anti-OXCT1 Antibody (Center) at 1:2000 dilution
Lane 1: Jurkat whole cell lysates
Lane 2: HepG2 whole cell lysates
Lane 3: Hela whole cell lysates
Lane 4: human heart lysates
Lane 5: mouse heart lysates
Lane 6: rat heart lysates
Lysates/proteins at 20 ug per lane.

Secondary
Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution

Predicted band size : 56 kDa

Blocking/Dilution buffer: 5% NFDM/TBST.

56158

3-oxoacid CoA transferase 1

succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial

Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial

OXCT; SCOT; SCOT-s  [Similar Products]

SCOT1_HUMAN

This gene encodes a member of the 3-oxoacid CoA-transferase gene family. The encoded protein is a homodimeric mitochondrial matrix enzyme that plays a central role in extrahepatic ketone body catabolism by catalyzing the reversible transfer of coenzyme A from succinyl-CoA to acetoacetate. Mutations in this gene are associated with succinyl CoA:3-oxoacid CoA transferase deficiency. [provided by RefSeq, Jul 2008]

OXCT1: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate. Defects in OXCT1 are a cause of succinyl-CoA-3-ketoacid- CoA transferase deficiency (SCOTD). A disorder of ketone body metabolism, characterized by episodic ketoacidosis. Patients are usually asymptomatic between episodes. Belongs to the 3-oxoacid CoA-transferase family.

Protein type: Amino Acid Metabolism - valine, leucine and isoleucine degradation; Lipid Metabolism - synthesis and degradation of ketone bodies; Mitochondrial; EC 2.8.3.5; Transferase; Carbohydrate Metabolism - butanoate

Chromosomal Location of Human Ortholog: 5p13.1

Cellular Component: mitochondrion; mitochondrial matrix

Molecular Function: protein homodimerization activity; 3-oxoacid CoA-transferase activity

Biological Process: response to drug; response to starvation; response to ethanol; heart development; response to hormone stimulus; ketone body catabolic process; ketone catabolic process; response to activity; cellular lipid metabolic process; ketone body metabolic process; brain development; response to nutrient

Disease: Succinyl-coa:3-oxoacid Coa Transferase Deficiency

Kassovska-Bratinova S.,et al.Am. J. Hum. Genet. 59:519-528(1996).
Fukao T.,et al.Genomics 68:144-151(2000).
Schmutz J.,et al.Nature 431:268-274(2004).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Reymond M.A.,et al.Submitted (FEB-1997) to UniProtKB.

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