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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. Zusätzlich bieten wir Ihnen VDAC2 Proteine (3) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal VDAC2 Primary Antibody für ELISA, WB - ABIN268631
Blachly-Dyson, Zambronicz, Yu, Adams, McCabe, Adelman, Colombini, Forte: Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel. in The Journal of biological chemistry 1993
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Cow (Bovine) Polyclonal VDAC2 Primary Antibody für IHC, WB - ABIN2776154
Chandra, Choy, Daniel, Tang: Bax-dependent regulation of Bak by voltage-dependent anion channel 2. in The Journal of biological chemistry 2005
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The works available on VDAC cysteines support the notion that VDAC1 (zeige VDAC1 Antikörper), VDAC2, and VDAC3 (zeige VDAC3 Antikörper) proteins are paralogs with a similar pore-function and slightly different, but important, ancillary biological functions. (Review)
The evolutionary demand for the NTE (zeige PNPLA6 Antikörper) 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 (zeige BAK1 Antikörper) import and tBid-induced apoptosis.
Results show that in thyroid tumours and cell lines, VDAC2 is upregulated and BAK1 (zeige BAK1 Antikörper) downregulated. Also, transient knockdown of VDAC2 promoted upregulation of the BAK1 (zeige BAK1 Antikörper) expression, and increased susceptibility to sorafenib treatment.
These data suggest that an interaction between Mcl-1 (zeige MCL1 Antikörper) and VDAC promotes lung cancer cell migration by a mechanism that involves Ca(2 (zeige CA2 Antikörper)+)-dependent reactive oxygen species production.
RACK1 (zeige GNB2L1 Antikörper) plays an antiapoptotic role during IBDV infection via interaction with VDAC2 and VP5.
GSK-3beta (zeige GSK3b Antikörper) translocates from the cytosol to mitochondria in a kinase activity- and VDAC2-dependent manner in which an N-terminal domain of GSK-3beta (zeige GSK3b Antikörper) 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.
an important MYBL2 (zeige MYBL2 Antikörper)-VDAC2-BECN1 (zeige BECN1 Antikörper)-BCL2L1 (zeige BCL2L1 Antikörper) pathway linking autophagy suppression in the developing ovary, is reported.
Bax (zeige BAX Antikörper) localizes to the mitochondrial outer membrane via alternate mechanisms, either constitutively via an interaction with VDAC2 or after activation via interaction with Bcl-2 (zeige BCL2 Antikörper) family proteins.
Bcl-xL (zeige BCL2L1 Antikörper) interacts functionally with VDAC1 (zeige VDAC1 Antikörper) and -3 but not VDAC2.
VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK (zeige BAK1 Antikörper), thereby controlling tBID-induced OMM permeabilization and cell death.
VDAC2 regulates the activity of BAK (zeige BAK1 Antikörper) and provides a connection between mitochondrial physiology and the core apoptotic pathway
Vdacs are dispensable for both MPT and Bcl-2 (zeige BCL2 Antikörper) 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 (zeige BAK1 Antikörper) axis governs the homeostasis of thymocytes.
ENO1 (zeige ENO1 Antikörper), VDAC2, and UQCRC2 (zeige UQCRC2 Antikörper) 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 (zeige VDAC3 Antikörper) might have an alternative structural organization and different functions in outer dense fibers (zeige ODF1 Antikörper) 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.
These findings demonstrate a critical modulatory role for VDAC2-dependent mitochondrial Ca(2 (zeige CA2 Antikörper)+) 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 (zeige VDAC1 Antikörper) and 2 subtypes in GV (germinal vesicle) and MII (meiosis II) stage porcine oocytes as well as their protein expression.
AtVDAC2 has a main function in mitochondria
VDAC2 and VDAC4 are important for leaf development, the mitochondrial membrane potential, and pollen development.
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.
outer mitochondrial membrane protein porin 2
, voltage-dependent anion-selective channel protein 2
, voltage-dependent anion-selective channel protein 6
, voltage-dependent anion channel 2
, outer mitochondrial membrane protein porin