Rabbit anti-Human DLAT Polyclonal Antibody

Uniprot Id

P10515

Target Species

Human

Target Name

DLAT

Target Full Name

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Target Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.

Target Involvement

Pyruvate dehydrogenase E2 deficiency (PDHE2 deficiency)

Target Subcellular Location

Mitochondrion matrix.

Target Protein Families

2-oxoacid dehydrogenase family

Target Research Area

Metabolism

Target Synonyms

70 kDa mitochondrial autoantigen of primary biliary cirrhosis; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide S Acetyltransferase; Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex mitochondrial; DLAT; DLTA; E2; E2 component of pyruvate dehydrogenase complex; M2 antigen complex 70 kDa subunit; mitochondrial; ODP2_HUMAN; PBC; PDC E2; PDC-E2; PDCE2; Pyruvate dehydrogenase complex component E2; Pyruvate dehydrogenase complex E2 subunit

Target Background

This gene encodes component E2 of the multi-enzyme pyruvate dehydrogenase complex (PDC). PDC resides in the inner mitochondrial membrane and catalyzes the conversion of pyruvate to acetyl coenzyme A. The protein product of this gene, dihydrolipoamide acetyltransferase, accepts acetyl groups formed by the oxidative decarboxylation of pyruvate and transfers them to coenzyme A. Dihydrolipoamide acetyltransferase is the antigen for antimitochondrial antibodies. These autoantibodies are present in nearly 95% of patients with the autoimmune liver disease primary biliary cirrhosis (PBC). In PBC, activated T lymphocytes attack and destroy epithelial cells in the bile duct where this protein is abnormally distributed and overexpressed. PBC enventually leads to cirrhosis and liver failure. Mutations in this gene are also a cause of pyruvate dehydrogenase E2 deficiency which causes primary lactic acidosis in infancy and early childhood.