Dihydrolipoamide Dehydrogenase/DLD Antibody (1016619) [Alexa Fluor® 488]

• Reactivity: Hu
• Applications: IHC, ICC/IF
• Clone: 1016619
• Clonality: Monoclonal
• Host: Mouse
• Conjugate: Alexa Fluor 488

Dihydrolipoamide Dehydrogenase/DLD Antibody (1016619) [Alexa Fluor® 488] Summary

• Immunogen: E. coli-derived human Dihydrolipoamide Dehydrogenase/DLD
  Ala36-Phe509
  Accession # P09622
• Specificity: Detects human Dihydrolipoamide Dehydrogenase/DLD in direct ELISAs.
• Isotype: IgG2b
• Clonality: Monoclonal
• Host: Mouse
• Purity Statement: Protein A or G purified

Applications/Dilutions

• Dilutions:
  • Immunocytochemistry
  • Immunohistochemistry

Packaging, Storage & Formulations

• Storage: Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
• Buffer: Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Dihydrolipoamide Dehydrogenase/DLD Antibody (1016619) [Alexa Fluor® 488]

• 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex)
• branched chain keto acid dehydrogenase complex
• Diaphorase
• dihydrolipoamide dehydrogenase (E3 component of pyruvate dehydrogenase complex
• Dihydrolipoamide Dehydrogenase
• dihydrolipoamide dehydrogenasemitochondrial
• DLD
• DLDD
• DLDH
• E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex
• E3
• EC 1.8.1
• EC 1.8.1.4
• GCSL
• Glycine cleavage system L protein
• glycine cleavage system protein L
• LAD
• Lipoamide Dehydrogenase
• lipoamide reductase
• lipoyl dehydrogenase
• PHE3

Background

Dihydrolipoamide dehydrogenase (DLD), also known as LADH, is an NAD-dependent oxidoreductase in the mitochondrial matrix (1). DLD serves as the E3 subunit of four mitochondrial enzyme complexes: pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, branched chain alpha-ketotacid dehydrogenase, and the glycine cleavage system (2, 3). It is active as a 120 kDa dimer that catalyzes oxidation within these enzyme complexes. Several mutations of human DLD have been described, some of which contribute to the loss of respiratory function during oxidative stress (4, 5). DLD mutations located at the interface between dimer subunits can impair dimer formation (5, 6). The involvement of DLD in the regulation of lipid peroxidation and lactate metabolism is important for mouse hippocampal neuroblast proliferation and hamster sperm capacitation, respectively (7, 8). DLD polymorphisms in insects can increase their resistance to the pesticide phosphine gas, while they can increase the sensitivity to arsenite in the nematode C. elegans (9). Mature human DLD shares 95-96% amino acid (aa) sequence identity with hamster, mouse, and rat DLD. Alternative splicing generates additional human DLD isoforms that lack the N-terminal 99 aa or carry a deletion of aa 147-194.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.