VDAC1 | voltage-dependent anion-selective channel protein 1

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AS07 212  |  clonality: polyclonal  |  host: rabbit  |  reactivity: A.thaliana, di and monocots,| cellular [compartment marker] of mitochondrial outer membrane


47 st
Item No:
AS07 212

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product information

VDAC1 protein (called also Synonymes: At3g01280, outer mitochondrial membrane protein porin 1, T22N4_9, T22N4.9, VDAC 1, Voltage-dependent anion-selective channel protein 1, voltage-gated ion-selective channel) forms a channel through the cell membrane for diffusion of small hydrophilic molecules. Evolutionary origin of VDAC protein is not clear and their structure and properties are quite different making those proteins only conceptually like porins (Clausen et al. 2004).


KLH-conjugated peptide conserved in all known higher plant VDAC1 proteins including Arabidopsis thaliana with the locus name: At3g01280

Host Rabbit
Clonality Polyclonal
Purity Affinity purified serum
Format Lyophilized in PBS pH 7.4
Quantity 50 µg
Reconstitution For reconstitution add 50 ĩl of sterile water.

store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

Tested applications western blot (WB), Blue-native (2D BN/SDS-PAGE), immunolocalization (IL)
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collection of antibodies to other mitochondrial proteins

Additional information

cellular [compartment marker] of mitochondrial outer membrane

application information
Recommended dilution

1:5000 on 2-30 µg of protein/lane with standard ECL (WB),  1: 500 (IL)

Expected | apparent MW

29 kDa (for Arabidopsis thaliana)

Confirmed reactivity

Arabidopsis thaliana, Beta vulgaris, Brassica oleracea var. botrytis, Oryza sativa, Papaver sp. pollen tubes (IL), Spinacia oleracea, Physcomitrella patens

Predicted reactivity

Arabidopsis alpina, Aundo donax, Brachypodium distachyon, Brassica campestris, Brassica napus, Brassica rapa subsp. pekinensis,  Capsella rubella, Citrus clementina, Citrus sinensis, Eutrema salsugineum, Glycine max, Glycine soja, Gossypium arboreum, Hoedum vulgare var. distichum, Jatropha curcas, Medicago truncatula, Mesembryanthemum crystallinum,  Morus notabilis, Nicotiana tabacum, Phaseolus coccineus, Phaseolus vulgaris, Pisum sativum, Plantago major, Prunus persicaRicinus communis, Solanum lycopersicum, Solanum tuberosum, Sorghum bicolor, Theobroma cacao, Triticum aestivum, Vitis vinifera, Zea mays

Not reactive in

Chlamydomonas reinhardtii, Glycine max, Zea mays, diatoms, Saccharomyces cerevisiae

Additional information

Amount of mitochondrial fraction detected by anti-VDAC1 antibody was from 2-10 µg.

Immunolocalization method description and images are available here

Blue-native (2D BN/SDS-PAGE) methodology is described in Piechota et al. 2010

Selected references de Michele et al. (2016). Free-Flow Electrophoresis of Plasma Membrane Vesicles Enriched by Two-Phase Partitioning Enhances the Quality of the Proteome from Arabidopsis Seedlings. J Proteome Res. 2016 Mar 4;15(3):900-13. doi: 10.1021/acs.jproteome.5b00876. Epub 2016 Feb 4.
Li et al. (2015). A Chaperone Function of NO CATALASE ACTIVITY1 Is Required to Maintain Catalase Activity and for Multiple Stress Responses in Arabidopsis. Plant Cell. 2015 Feb 19. pii: tpc.114.135095.
Rurek et al. (2015). Biogenesis of mitochondria in cauliflower (Brassica oleracea var. botrytis) curds subjected to temperature stress and recovery involves regulation of the complexome, respiratory chain activity, organellar translation and ultrastructure. Biochim Biophys Acta. 2015 Jan 21. pii: S0005-2728(15)00016-X. doi: 10.1016/j.bbabio.2015.01.005.
Hsueh et al. (2014). The chloroplast outer envelope protein P39 in Arabidopsis thaliana belongs to the Omp85 protein family. Proteins. 2014 Nov 17. doi: 10.1002/prot.24725.
Takahashi et al. (2014). Transport of rice cyclobutane pyrimidine dimer (CPD) photolyase into mitochondria relies on a targeting sequence located in its C-terminal internal region.
Alcántar-Aguirre et al.(2013).ATP produced by oxidative phosphorylation is channeled toward hexokinase bound to mitochondrial porin (VDAC) in beetroots (Beta vulgaris). Planta, March 17.

application example

western blot using anti-VDAC1 antibodies

Crude membrane proteins were separated on 12% SDS-PAGE and blotted 1h to PVDF. Blots were blocked immediately following transfer in 5% blocking reagent (BioRad, 170-6404) in 50 mM Tris, 150 mM sodium chloride pH 7.5 with 0.1% (v/v) Tween-20 (TBS-T) for 1h at room temperature with agitation. Blots were incubated in the primary antibody in 1: 5000 dilution for over-night at 4°C with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed 3 times for 5 min in TBS-T at room temperature with agitation. Blots were incubated in secondary antibody (Goat anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:5000 in 0.2% blocking solution for 1h at room temperature with agitation. The blots were washed as above and developed for 1~2 min with ECL detection reagent (Western bright ECL, Advansta; K-12045-D10) according the manufacturers instructions. Images of the blots were obtained using a CCD imager (LAS4000 GE) and by ImageQuant software (GE).

Arabidopsis thaliana membrane extraction and SDS–PAGE analysis About 200 mg (gFW) Arabidopsis seedlings (3-week-old), grown on 1% MS-agar plates, was ground with mortar and pestle in the presence of 2 ml extraction buffer [75 mM MOPS-KOH, 0.6 M Sucrose, 4 mM EDTA, 0.2% PVP-40, 0.2% BSA, 8 mM L-cystein, pH 7.6] and the protease inhibitor cocktail ‘complete Mini’ from Roche Diagnostics GmbH (Mannheim, Germany). Crude membrane extracts were prepared essentially as described in Colas des Francs-Small et al. (2012). The membranous fraction was obtained by centrifugation at 22,000 g for 10 min at 4oC. The pellet containing the crude membranous fraction was washed twice with wash buffer [37.5 mM MOPS-KOH, 0.3 M Sucrose, 2 mM EDTA pH 7.6]. The samples were kept frozen at -80oC until used. For SDS-PAGE, an aliquot equivalent to 10 mg (i.e. 1x dilution) of crude Arabidopsis membrane extracts was solubilized in 3x Laemmli sample buffer (Bio-Rad) and the proteins were analyzed by SDS-gel electrophoresis.

Courtesy of Dr. Oren Ostersetzer, The Hebrew University of Jerusalem, Israel

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