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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 Proteins (3) and many more products for this protein.
Showing 10 out of 70 products:
Human Monoclonal VDAC2 Primary Antibody for WB - ABIN395945
De Pinto, Guarino, Guarnera, Messina, Reina, Tomasello, Palermo, Mazzoni: Characterization of human VDAC isoforms: a peculiar function for VDAC3? in Biochimica et biophysica acta 2010
Show all 5 references for ABIN395945
Human Polyclonal VDAC2 Primary Antibody for 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
Show all 2 references for ABIN268631
Cow (Bovine) Polyclonal VDAC2 Primary Antibody for EIA, IHC (p) - ABIN374420
Vilagran, Yeste, Sancho, Casas, Rivera del Álamo, Bonet: Relationship of sperm small heat-shock protein 10 and voltage-dependent anion channel 2 with semen freezability in boars. in Theriogenology 2014
Show all 2 references for ABIN374420
Chicken Polyclonal VDAC2 Primary Antibody for WB - ABIN2776154
Chandra, Choy, Daniel, Tang: Bax-dependent regulation of Bak by voltage-dependent anion channel 2. in The Journal of biological chemistry 2005
Show all 2 references for ABIN2776154
Chicken Polyclonal VDAC2 Primary Antibody for WB - ABIN2776155
Valis, Neubauerova, Man, Pompach, Vohradsky, Kovar: VDAC2 and aldolase A identified as membrane proteins of K562 cells with increased expression under iron deprivation. in Molecular and cellular biochemistry 2008
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 Antibodies), VDAC2, and VDAC3 (show VDAC3 Antibodies) 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 Antibodies) 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 Antibodies) import and tBid-induced apoptosis.
Results show that in thyroid tumours and cell lines, VDAC2 is upregulated and BAK1 (show BAK1 Antibodies) downregulated. Also, transient knockdown of VDAC2 promoted upregulation of the BAK1 (show BAK1 Antibodies) expression, and increased susceptibility to sorafenib treatment.
These data suggest that an interaction between Mcl-1 (show MCL1 Antibodies) and VDAC promotes lung cancer cell migration by a mechanism that involves Ca(2 (show CA2 Antibodies)+)-dependent reactive oxygen species production.
RACK1 (show GNB2L1 Antibodies) plays an antiapoptotic role during IBDV infection via interaction with VDAC2 and VP5.
GSK-3beta (show GSK3b Antibodies) translocates from the cytosol to mitochondria in a kinase activity- and VDAC2-dependent manner in which an N-terminal domain of GSK-3beta (show GSK3b Antibodies) 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 Antibodies), VDAC2, and UQCRC2 (show UQCRC2 Antibodies) 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 Antibodies) might have an alternative structural organization and different functions in outer dense fibers (show ODF1 Antibodies) 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 Antibodies)-VDAC2-BECN1 (show BECN1 Antibodies)-BCL2L1 (show BCL2L1 Antibodies) pathway linking autophagy suppression in the developing ovary, is reported.
Bax (show BAX Antibodies) 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 Antibodies) family proteins.
Bcl-xL (show BCL2L1 Antibodies) interacts functionally with VDAC1 (show VDAC1 Antibodies) and -3 but not VDAC2.
VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK (show BAK1 Antibodies), thereby controlling tBID-induced OMM permeabilization and cell death.
VDAC2 regulates the activity of BAK (show BAK1 Antibodies) and provides a connection between mitochondrial physiology and the core apoptotic pathway
Vdacs are dispensable for both MPT and Bcl-2 (show BCL2 Antibodies) 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 Antibodies) axis governs the homeostasis of thymocytes.
These findings demonstrate a critical modulatory role for VDAC2-dependent mitochondrial Ca(2 (show CA2 Antibodies)+) 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 Antibodies) 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