Anti-VDAC/Porin/VDAC1 Antibody Picoband® Fluoro647 Conjugated

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.

Voltage-dependent anion-selective channel protein 1; VDAC-1; hVDAC1; Outer mitochondrial membrane protein porin 1; Plasmalemmal porin; Porin 31HL; Porin 31HM; VDAC1; VDAC

A synthetic peptide corresponding to a sequence in the middle region of human VDAC/Porin, different from the related mouse and rat sequences by one amino acid.

Cancer, Metabolism, Mitochondria, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Organelles, Pathways and Processes, Signal Transduction, Subcellular Markers, Tags & Cell Markers

Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. .

1. Blachly-Dyson, E., Zambronicz, E. B., Yu, W. H., Adams, V., McCabe, E. R. B., Adelman, J., Colombini, M., Forte, M.Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel.J. Biol. Chem. 268: 1835-1841, 1993. 2. Geisler, S., Holmstrom, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., Springer, W.PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1.Nature Cell Biol. 12: 119-131, 2010. 3. Huizing, M., Ruitenbeek, W., van den Heuvel, L. P., Dolce, V., Iacobazzi, V., Smeitink, J. A. M., Palmieri, F., Trijbels, J. M. F.Human mitochondrial transmembrane metabolite carriers: tissue distribution and its implication for mitochondrial disorders.J. Bioenerg. Biomembr. 30: 277-284, 1998.