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VDAC2 encodes a member of the voltage-dependent anion channel pore-forming family of proteins that are considered the main pathway for metabolite diffusion across the mitochondrial outer membrane. Additionally we are shipping VDAC2 Antibodies (70) and VDAC2 Proteins (3) and many more products for this protein.
AtVDAC2 has a main function in mitochondria
VDAC2 and VDAC4 are important for leaf development, the mitochondrial membrane potential, and pollen development.
The works available on VDAC cysteines support the notion that VDAC1 (show VDAC1 ELISA Kits), VDAC2, and VDAC3 (show VDAC3 ELISA Kits) proteins are paralogs with a similar pore-function and slightly different, but important, ancillary biological functions. (Review)
The evolutionary demand for the NTE (show PNPLA6 ELISA Kits) in the presence of cysteines clearly emerges from our biochemical and functional studies, providing insight into factors that functionally demarcate hVDAC-2 from the other VDACs.
Motifs of VDAC2 required for mitochondrial Bak (show BAK1 ELISA Kits) import and tBid-induced apoptosis.
Results show that in thyroid tumours and cell lines, VDAC2 is upregulated and BAK1 (show BAK1 ELISA Kits) downregulated. Also, transient knockdown of VDAC2 promoted upregulation of the BAK1 (show BAK1 ELISA Kits) expression, and increased susceptibility to sorafenib treatment.
These data suggest that an interaction between Mcl-1 (show MCL1 ELISA Kits) and VDAC promotes lung cancer cell migration by a mechanism that involves Ca(2 (show CA2 ELISA Kits)+)-dependent reactive oxygen species production.
RACK1 (show GNB2L1 ELISA Kits) plays an antiapoptotic role during IBDV infection via interaction with VDAC2 and VP5.
GSK-3beta translocates from the cytosol to mitochondria in a kinase activity- and VDAC2-dependent manner in which an N-terminal domain of GSK-3beta may function as a mitochondrial targeting sequence
Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial beta-barrel anion channel VDAC-2.
minor conformational variations in local residues are sufficient to define the membrane protein dynamics in hVDAC-2.
The reconstitution of functional VDAC-2 in lauryldimethylamine-oxide (LDAO) detergent micelles and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) lipid bilayer nanodiscs, is reported.
ENO1 (show ENO1 ELISA Kits), VDAC2, and UQCRC2 (show UQCRC2 ELISA Kits) were significantly correlated with individual fertility in bulls.
Results describe the expression of voltage-dependent anion channel isoforms in rat, bovine, and chicken brain mitochondria, and suggest that the nature of hexokinase binding site is not determined by the expression of a single VDAC isoform.
VDAC2 and VDAC3 (show VDAC3 ELISA Kits) might have an alternative structural organization and different functions in outer dense fibers (show ODF1 ELISA Kits) than in mitochondria
Confirm the localisation of VDAC2 in the acrosomal region of bovine spermatozoa using immunoelectron microscopy.
The present study is the first work to report the purification and characterization of VDAC2 from a mammalian tissue.
an important MYBL2 (show MYBL2 ELISA Kits)-VDAC2-BECN1 (show BECN1 ELISA Kits)-BCL2L1 (show BCL2L1 ELISA Kits) pathway linking autophagy suppression in the developing ovary, is reported.
Bax (show BAX ELISA Kits) localizes to the mitochondrial outer membrane via alternate mechanisms, either constitutively via an interaction with VDAC2 or after activation via interaction with Bcl-2 (show BCL2 ELISA Kits) family proteins.
Bcl-xL (show BCL2L1 ELISA Kits) interacts functionally with VDAC1 (show VDAC1 ELISA Kits) and -3 but not VDAC2.
VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK (show BAK1 ELISA Kits), thereby controlling tBID-induced OMM permeabilization and cell death.
VDAC2 regulates the activity of BAK (show BAK1 ELISA Kits) and provides a connection between mitochondrial physiology and the core apoptotic pathway
Vdacs are dispensable for both MPT and Bcl-2 (show BCL2 ELISA Kits) family member-driven cell death.
Genetic depletion of Vdac2 in the thymus resulted in excessive cell death & hypersensitivity to diverse death stimuli including engagement of the T cell receptor. The VDAC2-BAK (show BAK1 ELISA Kits) axis governs the homeostasis of thymocytes.
These findings demonstrate a critical modulatory role for VDAC2-dependent mitochondrial Ca(2 (show CA2 ELISA Kits)+) uptake in the regulation of cardiac rhythmicity.
Data indicate the structure of voltage-dependent anion channel 2 zfVDAC2 at 2.8 A resolution, revealing a crystallographic dimer.
Data confirm the synthesis of VDAC1 (show VDAC1 ELISA Kits) and 2 subtypes in GV (germinal vesicle) and MII (meiosis II) stage porcine oocytes as well as their protein expression.
This gene encodes a member of the voltage-dependent anion channel pore-forming family of proteins that are considered the main pathway for metabolite diffusion across the mitochondrial outer membrane. The encoded protein is also thought to be involved in the mitochondrial apoptotic pathway via regulation of BCL2-antagonist/killer 1 protein activity. Pseudogenes have been identified on chromosomes 1, 2, 12 and 21, and alternative splicing results in multiple transcript variants.
voltage-dependent anion channel 2
, voltage-dependent anion-selective channel protein 2
, outer mitochondrial membrane protein porin 2
, voltage-dependent anion-selective channel protein 6
, outer mitochondrial membrane protein porin