VDAC1-5 | Voltage-dependent anion-selective channel protein 1-5

AS07 212  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: A. thaliana, di and monocots | Cellular [compartment marker] of mitochondrial outer membrane

VDAC1-5 | Voltage-dependent anion-selective channel protein 1-5 in the group Antibodies for Plant/Algal  / Arabidopsis thaliana  at Agrisera AB (Antibodies for research) (AS07 212)


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Product Information


KLH-conjugated peptide conserved in all known higher plant VDAC proteins including Arabidopsis thaliana VDAC1 UniProt: Q9SRH5 , TAIR: AT3G01280, VDAC2  UniProt F4K3R8-1 , TAIR: AT5G67500, VDAC3 UniProt: Q9SMX3-1, TAIR: AT5G15090,     VDAC4 UniProt: Q9FKM2-1, TAIR:AT5G57490, VDAC5 UniProt: Q9M2W6-1, TAIR: AT3G49920 

Host Rabbit
Clonality Polyclonal
Purity Affinity purified serum in PBS pH 7,4
Format Lyophilized
Quantity 50 µg
Reconstitution For reconstitution add 50 ĩl of sterile water
Storage 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 Blue Native PAGE (2D BN/SDS-PAGE), Western blot (WB)
Recommended dilution 1 : 500 (IL), 1 : 5000,2-30 µg protein/lane (WB)
Expected | apparent MW

29 kDa (for Arabidopsis thaliana)


Confirmed reactivity Arabidopsis thaliana, Beta vulgaris, Brassica oleracea var. botrytis, Brassica rapa subsp. rapa, Citrus sinensis, Fortunella margarita Swingle, Oryza sativa, Papaver sp. pollen tubes (IL), Spinacia oleracea, Physcomitrella patens, Zea mays
Predicted reactivity

Arabidopsis alpina, Aundo donax, Brachypodium distachyon, Brassica campestris, Brassica napus, Brassica rapa subsp. pekinensis,  Capsella rubella, Citrus clementina, 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

Species of your interest not listed? Contact us
Not reactive in

Chlamydomonas reinhardtii, Glycine max, diatoms, Saccharomyces cerevisiae

Application examples

Application examples
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 chemiluminescent detection reagent, 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

VDAC1 confocal image

Fixation and Immunolocalization

(A) full confocal stacks; (B) Single confocal section
Pollen tubes were fixed in 400 μM 3-maleimodobenzoic acid N-hydroxysuccinimide ester (MBS, Pierce) for 6 min at 20ºC, followed by 2% formaldehyde  (1 h, 4°C). Cells were washed three times in 1x TBS then once in MES buffer (15 mM MES, pH 5.0), then incubated in 0.05% cellulose/0.05% macerozyme with 0.1% Triton X-100 in MES buffer containing 0.1 mM PMSF and 1 % BSA for 15 min. Cells were washed once in MES, then twice in TBS and then incubated in blocking solution (1% BSA in TBS) for 30 min at room temperature. Pollen was incubated with anti-VDAC1 antibodyies diluted in blocking solution (at 1:500) overnight at 4°C. Following TBS washes pollen was then incubated with the secondary antibody for 1.5 h at room temperature followed by further TBS washes. Pollen tubes were mounted on slides with 5 μL of Vectashield + DAPI (Vector Laboratories, USA) and coverslips sealed with nail varnish.

Method taken from Poulter et al (submitted) Actin-binding proteins implicated in formation of the punctate actin foci stimulated by the self-incompatibility response in Papaver . Submitted to Plant Physiology.

Courtesy Professor Noni Franklin-Tong, University of Birmingham, UK

Additional information

Additional information Cellular [compartment marker] of mitochondrial outer membrane for western blot,
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

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VDAC proteins are porin-type, beta-barrel diffusion pores. Prominently localized in the outer mitochondrial membrane and involved in metabolite exchange. 

Product citations

Selected references Li et al. (2021) Isolation and comparative proteomic analysis of mitochondria from the pulp of ripening citrus fruit. Hortic Res. 2021 Feb 1;8(1):31. doi: 10.1038/s41438-021-00470-w. PMID: 33518707; PMCID: PMC7848011.
Tarasenko et al. (2020). Plant mitochondrial subfractions have different ability to import DNA. Theor. Exp. Plant Physiol.
Garmash et al. (2020). Altered levels of AOX1a expression result in changes in metabolic pathways in Arabidopsis thaliana plants acclimated to low dose rates of ultraviolet B radiation. Plant Sci. 2020 Feb;291:110332. doi: 10.1016/j.plantsci.2019.110332.
Bai et al. (2019). Overexpression of soybean GmPLD? enhances seed oil content and modulates fatty acid composition in transgenic Arabidopsis. Plant Science Volume 290, January 2020, 110298.
Klinger et al. (2019). The signal distinguishing between targeting of outer membrane ß-barrel protein to plastids and mitochondria in plants. Biochim Biophys Acta Mol Cell Res. 2019 Jan 8;1866(4):663-672. doi: 10.1016/j.bbamcr.2019.01.004.
Zhu et al. (2018). A comprehensive proteomic analysis of elaioplasts from citrus fruits reveals insights into elaioplast biogenesis and function. Hortic Res. 2018 Feb 7;5:6. doi: 10.1038/s41438-017-0014-x.
Kang et al. (2018). Autophagy-related (ATG) 11, ATG9 and the phosphatidylinositol 3-kinase control ATG2-mediated formation of autophagosomes in Arabidopsis. Plant Cell Rep. 2018 Jan 19. doi: 10.1007/s00299-018-2258-9.
Wang and Auwerx (2017). Systems Phytohormone Responses to Mitochondrial Proteotoxic Stress. Mol Cell. 2017 Nov 2;68(3):540-551.e5. doi: 10.1016/j.molcel.2017.10.006.
Yin et al. (2016). Comprehensive Mitochondrial Metabolic Shift during the Critical Node of Seed Ageing in Rice. PLoS One. 2016 Apr 28;11(4):e0148013. doi: 10.1371/journal.pone.0148013. eCollection 2016.
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.
Armbruster et al. (2014). Ion antiport accelerates photosynthetic acclimation in fluctuating light environments. Nat Commun. 2014 Nov 13;5:5439. doi: 10.1038/ncomms6439
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.

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