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Validated All-in-One™ qPCR Primer for VDAC1(NM_003374.2) Search again
Product ID:
HQP018470
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
PORIN, VDAC-1
Gene Description:
voltage dependent anion channel 1
Target Gene Accession:
NM_003374.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Gene References into function
- interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74; results of this study represent additional evidence of membrane-associated trafficking of the voltage-dependent anion-selective channel 1
- Activation of mitochondrial voltage-dependent anion channel by apro-apoptotic protein Bim
- Presence of a plasma membrane VDAC was demonstrated. Colocalisation of VDAC with caveolin-1.
- is a receptor for plasminogen kringle 5 on endothelial cells
- Identification of the protein-protein contact site and interaction mode of VDAC1 with Bcl-2 family proteins.
- a major function of VDAC1 in the plasma membrane is that of a NADH(-ferricyanide) reductase that may be involved in the maintenance of cellular redox homeostasis
- VDAC homodimerization could potentially determine its gating capacity to cyto c, and Bcl-2 blockage of VDAC homodimerization represents a novel mechanism for its inhibition of apoptosis.
- a model on how electron transport may occur in VDAC1.
- evidences of VDAC-COX interaction in vitro proved to be functional as evidenced by the effect of the human and yeast isoforms of VDAC on the oxidation of cytochrome c by the pure holoenzyme and by the effect of the COX epitope on VDAC permeability
- VDAC1 regulates apoptosis independent of the apoptosis-inducing pathway.
- Bcl-xL can bind to one or two VDAC1 molecules forming heterodimers and heterotrimers.
- gelsolin G5 domain inhibits HIV-Vpr-induced T-cell apoptosis by blocking the interaction between Vpr and VDAC
- hVDAC1 formed different structures in detergent micelles and phospholipid bilayers.
- Our analysis strongly suggests a 16-stranded, antiparallel beta-barrel with one large and seven short loops and turns. Initial crystallization trials of the protein yielded crystals diffracting to 8 Angstrom resolution.
- phosphorylated StAR interacts with voltage-dependent anion channel 1 (VDAC1) on the OMM, which then facilitates processing of the 37-kDa phospho-StAR to the 32-kDa intermediate.
- interference with the binding of Hexokinase-I to mitochondria by VDAC1-derived peptides may offer a novel strategy by which to potentiate the efficacy of conventional chemotherapeutic agents
- VDAC1 may act as a facultative regulator/effector of MMP, depending on the initial cytotoxic event.
- two serine residues of VDAC1, Ser-12 and Ser-103, can modulate VDAC1 protein level and thus the sensitivity to apoptosis stimuli
- High-resolution structure analysis of human VDAC1 crystal lattice reveals that it belongs to trigonal space group P321, with unit-cell parameters a = 78.9, c = 165.7 A and one monomer in the asymmetric unit.
- study presents NMR solution structure of recombinant VDAC-1 reconstituted in detergent micelles
- the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography