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$( A ) Scheme illustrating the biochemical purification of a light-weight membrane fraction enriched for myelin by homogenizing mouse brains in 0.32 M sucrose, sequential sucrose density gradient centrifugation, and osmotic shocks. Myelin accumulates at the interface between 0.32 M and 0.85 M sucrose. ( B ) Immunoblot analysis of myelin-enriched fractions and equal amounts of brain lysate to compare the abundance of marker proteins for compact myelin (PLP/DM20, MBP), non-compact myelin (CNP, SIRT2), the oligodendroglial nuclear/cytoplasmic compartment (OLIG2), astrocytes (GFAP), microglia (AIF1/IBA1), neuronal plasma <t>membrane</t> <t>(GPM6A),</t> axonal microtubules (TUBB3/TUJ1), and mitochondria <t>(VDAC).</t> Blot represents three biological replicates (male c57Bl6/N mice, age P75). Note that myelin markers were enriched in purified myelin while markers of other cellular sources were reduced. ( C ) Heatmap displaying reverse CT values from qRT-PCRs for three markers each specific for myelin, migroglia, neurons and astrocytes performed on myelin biochemically purified from the brains of 4 individual mice (M1–4) compared to the respective brain lysates (BL1–4) at six month of age.$
Vdac, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 91/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+vdac1+rabbit/pmc04865983-124-59-60?v=Rockland+Immunochemicals
Average 91 stars, based on 9 article reviews

vdac - by Bioz Stars, 2026-08

91/100 stars

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1) Product Images from "The transcriptome of mouse central nervous system myelin"

Article Title: The transcriptome of mouse central nervous system myelin

Journal: Scientific Reports

doi: 10.1038/srep25828

$( A ) Scheme illustrating the biochemical purification of a light-weight membrane fraction enriched for myelin by homogenizing mouse brains in 0.32 M sucrose, sequential sucrose density gradient centrifugation, and osmotic shocks. Myelin accumulates at the interface between 0.32 M and 0.85 M sucrose. ( B ) Immunoblot analysis of myelin-enriched fractions and equal amounts of brain lysate to compare the abundance of marker proteins for compact myelin (PLP/DM20, MBP), non-compact myelin (CNP, SIRT2), the oligodendroglial nuclear/cytoplasmic compartment (OLIG2), astrocytes (GFAP), microglia (AIF1/IBA1), neuronal plasma membrane (GPM6A), axonal microtubules (TUBB3/TUJ1), and mitochondria (VDAC). Blot represents three biological replicates (male c57Bl6/N mice, age P75). Note that myelin markers were enriched in purified myelin while markers of other cellular sources were reduced. ( C ) Heatmap displaying reverse CT values from qRT-PCRs for three markers each specific for myelin, migroglia, neurons and astrocytes performed on myelin biochemically purified from the brains of 4 individual mice (M1–4) compared to the respective brain lysates (BL1–4) at six month of age.$
Figure Legend Snippet: ( A ) Scheme illustrating the biochemical purification of a light-weight membrane fraction enriched for myelin by homogenizing mouse brains in 0.32 M sucrose, sequential sucrose density gradient centrifugation, and osmotic shocks. Myelin accumulates at the interface between 0.32 M and 0.85 M sucrose. ( B ) Immunoblot analysis of myelin-enriched fractions and equal amounts of brain lysate to compare the abundance of marker proteins for compact myelin (PLP/DM20, MBP), non-compact myelin (CNP, SIRT2), the oligodendroglial nuclear/cytoplasmic compartment (OLIG2), astrocytes (GFAP), microglia (AIF1/IBA1), neuronal plasma membrane (GPM6A), axonal microtubules (TUBB3/TUJ1), and mitochondria (VDAC). Blot represents three biological replicates (male c57Bl6/N mice, age P75). Note that myelin markers were enriched in purified myelin while markers of other cellular sources were reduced. ( C ) Heatmap displaying reverse CT values from qRT-PCRs for three markers each specific for myelin, migroglia, neurons and astrocytes performed on myelin biochemically purified from the brains of 4 individual mice (M1–4) compared to the respective brain lysates (BL1–4) at six month of age.

Techniques Used: Purification, Membrane, Gradient Centrifugation, Western Blot, Marker, Clinical Proteomics

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$( A ) Wild-type HEK293 and STIM1-KO cells were subjected to MAM fractionation, and TH, CM, MAM, and ER fractions were analyzed by immunoblotting (5 μg protein/lane). ACSL4 was used as a loading control for MAM fraction. ( B – D ) Enrichment of IP3Rs in the MAM fraction was quantified relative to total ER levels (MAM + ER signals). Data were normalized to the WT condition and plotted as mean ± S.D. from n = 5 biological replicates for IP3R3 and IP3R2, and n = 3 biological replicates for IP3R1/2/3. Statistical analysis with unpaired t-test in all cases. ( E ) GRP75 and VDAC1 proteins levels were analyzed in the MAM fractions from WT HEK293 and STIM1-KO HEK293 cells. ACSL4 was used as a loading control. ( F , G ) Data were normalized to the WT condition and plotted as mean ± S.D. from n = 4 biological replicates. Statistical analysis with unpaired t-test, p = 0.0288 in ( F ), p = 0.0452 in ( G ). ( H ) Methanol-fixed HEK293 cells were incubated with the indicated primary antibodies (rabbit anti-VDAC1 and/or mouse anti-IP3R1/2/3) as well as the DNA probes rabbit-PLUS and mouse-MINUS. As negative controls, cells were incubated with individual primary antibodies. Representative images for all the conditions are shown. Scale bar = 10 μm. ( I ) Quantification of the assay from ( H ), with the number of cells analyzed indicated in parentheses. The black line represents the mean of the data. Statistical analysis with unpaired t-test, **** p < 0.0001, * p = 0.0139. .$

Journal: The EMBO Journal

Article Title: STIM1-containing contact sites promote direct calcium flux from the endoplasmic reticulum to mitochondria

doi: 10.1038/s44318-026-00700-8

Figure Lengend Snippet: ( A ) Wild-type HEK293 and STIM1-KO cells were subjected to MAM fractionation, and TH, CM, MAM, and ER fractions were analyzed by immunoblotting (5 μg protein/lane). ACSL4 was used as a loading control for MAM fraction. ( B – D ) Enrichment of IP3Rs in the MAM fraction was quantified relative to total ER levels (MAM + ER signals). Data were normalized to the WT condition and plotted as mean ± S.D. from n = 5 biological replicates for IP3R3 and IP3R2, and n = 3 biological replicates for IP3R1/2/3. Statistical analysis with unpaired t-test in all cases. ( E ) GRP75 and VDAC1 proteins levels were analyzed in the MAM fractions from WT HEK293 and STIM1-KO HEK293 cells. ACSL4 was used as a loading control. ( F , G ) Data were normalized to the WT condition and plotted as mean ± S.D. from n = 4 biological replicates. Statistical analysis with unpaired t-test, p = 0.0288 in ( F ), p = 0.0452 in ( G ). ( H ) Methanol-fixed HEK293 cells were incubated with the indicated primary antibodies (rabbit anti-VDAC1 and/or mouse anti-IP3R1/2/3) as well as the DNA probes rabbit-PLUS and mouse-MINUS. As negative controls, cells were incubated with individual primary antibodies. Representative images for all the conditions are shown. Scale bar = 10 μm. ( I ) Quantification of the assay from ( H ), with the number of cells analyzed indicated in parentheses. The black line represents the mean of the data. Statistical analysis with unpaired t-test, **** p < 0.0001, * p = 0.0139. .

Article Snippet: Rabbit anti-VDAC1 (1:300 in blocking buffer, for IF) , Proteintech , 55259-1-AP.

Techniques: Fractionation, Western Blot, Control, Incubation