Anti vdac2

Manufactured by Abcam

Sourced in China

Anti-VDAC2 is a primary antibody that specifically recognizes the voltage-dependent anion channel 2 (VDAC2) protein. VDAC2 is a mitochondrial outer membrane protein that plays a role in regulating cellular metabolism and apoptosis. This antibody can be used for applications such as Western blotting and immunohistochemistry to detect and analyze VDAC2 expression in various samples.

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3 protocols using anti vdac2

Plasmid Construction and Antibody Details

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Plasmids expressing cMyc-tagged mouse SEPN1 (with A1284T/C conversion of the TGA selenocysteine codon into Cys to increase expression) and cMyc-tagged human Desmin were constructed in a CMV promoter-derived mammalian expression vector.
Expression plasmids encoding N-terminally FLAG-tagged human SEPN1 and the mutants SEPN1 SS (C427S, U428S) and SEPN1 CC (U428C) were constructed in pSel-Express vector (a kind gift from Vladimir Gladyshev) [16 ].
The primary antibodies used were: anti-VDAC2, anti-Cyt C, anti-Calnexin, anti-SERCA2, anti-RyR, anti-cMyc, and anti-PDI from Abcam; anti-Flag, anti-β-tubulin, and anti-Sigma 1-R from Sigma-Aldrich; anti-IP3R3 and Cyt c from BD Biosciences; anti-Tom40 from Santa Cruz, and homemade rabbit anti-SEPN1 [21 (link)]. Secondary antibodies Alexa Fluor 488 and 594 were from Life Technologies.

Filipe A., Chernorudskiy A., Arbogast S., Varone E., Villar-Quiles R.N., Pozzer D., Moulin M., Fumagalli S., Cabet E., Dudhal S., De Simoni M.G., Denis R., Vadrot N., Dill C., Giovarelli M., Szweda L., De Palma C., Pinton P., Giorgi C., Viscomi C., Clementi E., Missiroli S., Boncompagni S., Zito E, & Ferreiro A. (2020). Defective endoplasmic reticulum-mitochondria contacts and bioenergetics in SEPN1-related myopathy. Cell Death and Differentiation, 28(1), 123-138.

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Western Blot Analysis of Protein Expression

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Equal amounts of extracts (20 μg) were separated by 10% SDS‒PAGE and transferred to PVDF membranes. After blocking with 5% milk in TBST, the following specific primary antibodies were used: anti-G6PD (1:1000; Abcam, UK), anti-VDAC1 (1:1000; Abcam), anti-Bax (1:2000; Abways, China), anti-Bcl-2 (1:500; Abways), anti-SM22α (1:2000; Abcam), anti-PCNA (1:1000; Abcam), anti-VDAC2 (1:1000; Abcam), anti-VDAC3 (1:500; Wanlei bio, China), anti-β-actin (1:1000; PTM bio, China), anti-α-actin (1:1000; PTM bio), anti-GAPDH (1:1000; Proteintech, China), anti-Tom40 (1:1000; Proteintech), anti-Caspase 9 (1:1000; PTM bio), anti-Cleaved Caspase 9 (1:1000; Wanlei bio), anti-Caspase 7 (1:1000; PTM bio), anti-cleaved Caspase 7 (1:1000; Wanlei bio), anti-Caspase 3/Cleaved Caspase 3 (1:1000; Wanlei bio), and anti-PARP/Cleaved PARP (1:1000; Wanlei bio), and incubated at 4 °C overnight. The blots were visualized using a GE ImageQuant™ LAS 4000 detection system (USA). Band intensities were quantified with ImageJ software (USA).

Zhang T., Cao R.J., Niu J.L., Chen Z.H., Mu S.Q., Cao T., Pang J.X, & Dong L.H. (2024). G6PD maintains the VSMC synthetic phenotype and accelerates vascular neointimal hyperplasia by inhibiting the VDAC1–Bax-mediated mitochondrial apoptosis pathway. Cellular & Molecular Biology Letters, 29, 47.

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Hippocampal Protein Expression Analysis

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Rats were euthanized with an overdose of inhalative isoflurane and the brain rapidly removed. Frozen hippocampal tissues were homogenized in lysis buffer (50 mM Tris-HCl, 150 mM NaCl, 1% NP-40, 0.5% sodium deoxycholate, 0.1% SDS and protease and phosphatase cocktail inhibitor, pH 7.5) Total amounts of 15 µg protein per sample were separated on 10% sodium 4–15% Mini-Protean TGX Precast gels, and transferred to nitrocellulose membranes (BioRad Laboratories). After blocking, membranes were incubated overnight at 4°C with primary antibodies to VDAC1 and VDAC2 (anti-VDAC1 1:7,500, Abcam and anti-VDAC2 1:7,500 Abcam). The membranes were washed and incubated with horseradish peroxidase (HRP)-conjugated secondary antibodies (GE Healthcare) 1 hour at room temperature. Blots were developed with electrochemiluminescence (ECL Prime, GE Healthcare) and imaged on Kodak Molecular imaging system including analysis with ImageJ Gel Analysis software. All samples were run in one blot for each marker and β-actin was used as a loading standard. Protein levels were normalized to β-actin levels in the respective blots.

Rosenberger D.S., Falangola M.F., Ledreux A., Nie X., Suhre W.M., Boger H.A, & Granholm A.C. (2016). MEMORY AND HIPPOCAMPAL ARCHITECTURE FOLLOWING SHORT-TERM MIDAZOLAM IN WESTERN DIET-TREATED RATS. Neuroscience letters, 621, 68-74.

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