The voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane is a small, abundant outer membrane pore-forming protein found in the outer membranes of all eukaryotic mitochondria. The VDAC protein is thought to form the major pathway for movement of adenine nucleotides through the outer membrane and to be the mitochondrial binding site for hexokinase and glycerol kinase. At low transmembrane voltage, VDAC is open for anions such as phosphate, chloride, and adenine nucleotides. At higher transmembrane voltage, VDAC functions as a selective channel for cations and uncharged molecules. These features make VDAC likely to play a role in mitochondrial energy metabolism. Huizing et al. studied by Northern and Western blot analyses the human tissue distribution of mitochondrial transmembrane metabolite carriers. They found that VDAC1 mRNA has a ubiquitous distribution, with most pronounced expression in heart, liver, and skeletal muscle, whereas the VDAC2 isoform appears to be expressed only in the heart.

Optimal dilution of the VDAC antibody should be determined by the researcher.

Amino acids QMNFETAKSRVTQSNFAVGYKTDEFQLH of human VDAC/Porin were used as the immunogen for the VDAC antibody.

After reconstitution, the VDAC antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.