VDAC1 / 2 / 3 Recombinant Rabbit Monoclonal Antibody - BSA and Azide free [PSH14-90] (HA751534)

UNIPROT #

P21796

PROTEIN NAME

VDAC1 / 2 / 3

SYNONYMS

hVDAC1 antibody;MGC111064 antibody;Mithocondrial porin antibody;OPM2, yeast, human complement of antibody;Outer mitochondrial membrane protein porin 1 antibody;Plasmalemmal porin antibody;Porin 31 HL antibody;Porin 31 HM antibody;Porin 31HL antibody;Porin 31HM antibody;Porin antibody;VDAC 1 antibody;VDAC antibody;VDAC-1 antibody;Vdac1 antibody;VDAC1_HUMAN antibody;Voltage Dependent Anion Channel 1 antibody;voltage dependent anion selective channel protein 1 antibody;Voltage-dependent anion-selective channel protein 1 antibody;B-36 vdac antibody;FLJ23841 antibody;hVDAC2 antibody;OTTHUMP00000019878 antibody;OTTHUMP00000019879 antibody;OTTHUMP00000019880 antibody;Outer mitochondrial membrane protein porin 2 antibody;POR antibody;Porin-2 antibody;VDAC 2 antibody;VDAC-2 antibody;VDAC2 antibody;VDAC2_HUMAN antibody;Vdac6 antibody;Voltage dependent anion channel 2 antibody;Voltage dependent anion selective channel protein 2 antibody;Voltage-dependent anion-selective channel protein 2 antibody;Non-selective voltage-gated ion channel VDAC3;VDAC-3; hVDAC3;Outer mitochondrial membrane protein porin 3;VDAC3

SUBCELLULAR LOCATION

Mitochondrion outer membrane, Membrane.

FUNCTION

Voltage-dependent anion channels, or mitochondrial porins, are a class of porin ion channel located on the outer mitochondrial membrane. Humans, like most higher eukaryotes, encode three different VDACs; VDAC1, VDAC2, and VDAC3. Together with TOMM40 and TOMM40L they represent a family of evolutionarily related β-barrels. VDAC has also been shown to play a role in apoptosis. During apoptosis, VDAC modifies the mitochondrial permeability transition pore to release of apoptogenic factors such as cytochrome c. However, VDAC are not essential components of the mitochondrial permeability transition pore. Although cytochrome c plays an essential role in oxidative phosphorylation within the mitochondrion. In the cytosol it activates proteolytic enzymes called caspases, which play a major role in cell death. Although the mechanism for VDAC-facilitated cytochrome c release has not yet been fully elucidated, some research suggests that oligomerization between individual subunits may create a large flexible pore through which cytochrome c can pass. A more important factor is that release of cytochrome c is also regulated by the Bcl-2 protein family: Bax interacts directly with VDAC to increase pore size and promote cytochrome c release, while anti-apoptotic Bcl-xL produces the exact opposite effect. In fact, it has been shown that antibodies that inhibit VDAC also interfere with Bax-mediated cytochrome c release in both isolated mitochondria and whole cells. This key role in apoptosis suggests VDAC as a potential target for chemotherapeutic drugs.