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Anti porin

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Anti-Porin is a lab equipment product that functions as a marker for mitochondrial outer membrane proteins. It is commonly used in Western blotting and immunocytochemistry applications to detect and quantify the presence of porin, a protein involved in the permeability of the mitochondrial outer membrane.

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Lab products found in correlation

Anti β actin, by Merck Group (1 mentions) Gapdh, by HyTest (1 mentions) Horseradish peroxidase conjugated secondary antibody, by Southern Biotech (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Anti gapdh, by Thermo Fisher Scientific (1 mentions) Anti actin, by Developmental Studies Hybridoma Bank (1 mentions) Anti ha 11, by BioLegend (1 mentions) Anti pan akt, by Cell Signaling Technology (1 mentions) Anti pakt s473, by Cell Signaling Technology (1 mentions) Immobilon p membrane, by Merck Group (1 mentions) Trizol, by Thermo Fisher Scientific (1 mentions) Anti tubulin, by Merck Group (1 mentions) Anti ucp1, by Abcam (1 mentions) Anti actin, by Cell Signaling Technology (1 mentions) P creb, by Cell Signaling Technology (1 mentions) Total creb, by Cell Signaling Technology (1 mentions) Cell surface protein isolation kit, by Thermo Fisher Scientific (1 mentions) Peroxidase conjugated secondary antibody, by Bio-Rad (1 mentions) Anti nitrotyrosine antibody, by Merck Group (1 mentions) Anti pgp, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

Porin (15 citations) Anti-VDAC1/Porin (8 citations) Mouse anti-Porin (4 citations) Anti-porin antibody (4 citations) Rabbit anti-VDAC1/Porin (2 citations)

5 protocols using anti porin

1

Fractionation and Immunoblotting Protocols for Spinal Cord and Cultured Cells

Cited 1 time
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Fractionations experiments from spinal cord and cultured cells were performed as described (Niemann et al., 2009 (link); Li et al., 2010 (link)). Western blotting, detection and quantification were performed as described (Niemann et al., 2005 (link)). Antibodies: anti-GDAP1 (Niemann et al., 2005 (link)), anti-GDAP1L1 (Pineda; Supplementary material and Supplementary Fig. 4A), anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; HyTest), anti-Porin/voltage dependent anion channel (VDAC; Abcam) and anti-β-actin (Sigma).
Niemann A., Huber N., Wagner K.M., Somandin C., Horn M., Lebrun-Julien F., Angst B., Pereira J.A., Halfter H., Welzl H., Feltri M.L., Wrabetz L., Young P., Wessig C., Toyka K.V, & Suter U. (2014). The Gdap1 knockout mouse mechanistically links redox control to Charcot–Marie–Tooth disease. Brain, 137(3), 668-682.
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2

Western Blot Analysis of Metabolic Enzymes

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Western blots were performed as described previously [26 (link)]. The following antibodies were used: anti VLCAD (kindly provided by Dr S. Yamagushi, Japan), anti CPT2 (kindly provided by Dr C. Prip-Buus, France), anti porin (Abcam, Cambridge, UK), and anti ß-actin (Chemicon International, Temecula, USA). The bands were scanned by computerized densitometry (NIH Image J) and the results were expressed as arbitrary units, normalized to the amount of ß-actin.
Aires V., Delmas D., Le Bachelier C., Latruffe N., Schlemmer D., Benoist J.F., Djouadi F, & Bastin J. (2014). Stilbenes and resveratrol metabolites improve mitochondrial fatty acid oxidation defects in human fibroblasts. Orphanet Journal of Rare Diseases, 9, 79.
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3

Western Blot Analysis of Drosophila Proteins

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For western blot analysis, Drosophila heads were homogenized in 15 μl of 2X Laemmli’s buffer (Sigma-Aldrich). Samples were boiled for ten minutes and subjected to SDS-PAGE. Proteins were transferred to nitrocellulose membranes (Bio-Rad), blocked in 2% milk in PBS with 0.05% Tween 20, and immunoblotted following standard protocols. All immunoblots were repeated at least three times with similar results. The following antibodies were used: anti-synuclein (1:100,000, Developmental Studies Hybridoma Bank, H3C), anti-GAPDH (1:100000, Invitrogen), anti-actin (1:10000, Developmental Studies Hybridoma Bank, JLA20), anti-HA.11 (1:1000, BioLegend), anti-porin (1:50000, Abcam) and anti-α-spectrin (1:5000, Developmental Studies Hybridoma Bank, 3A9). The appropriate horseradish peroxidase-conjugated secondary antibody (SouthernBiotech) was applied, and signal was detected by chemiluminescence (Alpha Innotech). Ponceau S staining was used to monitor protein transfer and equivalent protein loading, which was also documented by reprobing with an antibody to GAPDH.
Ordonez D.G., Lee M.K, & Feany M.B. (2017). α-synuclein induces mitochondrial dysfunction through spectrin and the actin cytoskeleton. Neuron, 97(1), 108-124.e6.
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4

Quantifying mRNA and Protein Expression

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Total RNA from cultured cells or tissues was purified using TRIzol (Invitrogen) for cDNA synthesis (ABI High Capacity Reverse Transcription Kit). Relative mRNA expression was quantified by qPCR using SYBR Green dye (ABI) and specific primers (see Table S1 for primer sequences). For Western Blotting, whole cell lysates were prepared with RIPA buffer, separated by SDS-PAGE and transferred to ImmobilonP membranes (Millipore). The following antibodies were used: anti-CLK2 (NeoBioLab), anti-UCP1 (Abcam), pCREB (Cell Signaling), total CREB (Cell Signaling), anti-Tubulin (Milipore), anti-Lamin (Abcam), anti-Actin (Cell Signaling), anti-Porin (Abcam) anti-pAKT S473 (Cell Signaling), and anti-Pan AKT (Cell Signaling).
Hatting M., Rines A.K., Luo C., Tabata M., Sharabi K., Hall J.A., Verdeguer F., Trautwein C, & Puigserver P. (2017). Adipose tissue CLK2 promotes energy expenditure during high fat diet intermittent fasting. Cell metabolism, 25(2), 428-437.
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5

Plasma Membrane and Mitochondrial Protein Analysis

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Plasma-membrane-extracts were isolated by the biotination method, using the Cell Surface Protein isolation kit (Thermo Fisher Scientific Inc., Waltham, MA), as reported elsewhere 12 using an anti-pancadherin antibody (Santa Cruz Biotechnology Inc., Santa Cruz, CA) to check equal protein loading. Mitochondrial extracts were prepared as reported elsewhere, 8 using an anti-porin (Abcam) antibody to check equal loading of proteins. 50 µg proteins from plasma-membrane or 10 µg proteins from mitochondrial extracts were separated by SDS-PAGE and probed with the following antibodies: anti-Pgp (Santa Cruz Biotechnology), anti-MRP1 (Abcam, Cambridge, UK), and anti-BCRP (Santa Cruz Biotechnology). To analyze the presence of nitrated proteins, the mitochondrial extract was subjected to immunoprecipitation using a rabbit polyclonal anti-nitrotyrosine antibody (Millipore, Bedford, MA). Immunoprecipitated proteins were separated by SDS-PAGE and probed with anti-Pgp, anti-MRP1, and anti-BCRP antibodies. After overnight incubation, the membrane was washed with PBS-Tween 0.1% v/v and treated for 1 h with a peroxidase-conjugated secondary antibody (Bio-Rad Laboratories). The membrane was washed with PBS-Tween 0.1% v/v, and proteins were detected by enhanced chemiluminescence (Immun-Star, Bio-Rad Laboratories).
Gazzano E., Chegaev K., Rolando B., Blangetti M., Annaratone L., Ghigo D., Fruttero R, & Riganti C. (2016). Overcoming multidrug resistance by targeting mitochondria with NO-donating doxorubicins. Bioorganic & medicinal chemistry, 24(5).
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