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Criterion sds polyacrylamide gels

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The Criterion SDS polyacrylamide gels are a type of electrophoresis gel used for the separation and analysis of proteins. They provide a uniform and consistent matrix for the separation of proteins based on their molecular weight.

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Lab products found in correlation

Anti malonyl lysine, by PTM Biolabs (1 mentions) Anti β actin, by Proteintech (1 mentions) Anti acetyl lysine, by Cell Signaling Technology (1 mentions) Anti succinyllysine, by PTM Biolabs (1 mentions) Hsp60, by Cell Signaling Technology (1 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Enhanced chemiluminescence, by GE Healthcare (1 mentions) Sypro ruby staining, by Thermo Fisher Scientific (1 mentions) Anti c myc, by Cell Signaling Technology (1 mentions) Anti lamin a c, by Proteintech (1 mentions) Anti gapdh g8795, by Merck Group (1 mentions) Clarity max ecl, by Bio-Rad (1 mentions)

Close spelling variants of this product

Polyacrylamide gel (457 citations) SDS-polyacrylamide gel (334 citations) Criterion gels (84 citations) 10% SDS gel (31 citations) Criterion polyacrylamide gels (12 citations) Criterion precast SDS-polyacrylamide gels (2 citations) TGX Criterion gradient SDS polyacrylamide gels (2 citations)

4 protocols using criterion sds polyacrylamide gels

1

Western Blot Analysis of Protein Modifications

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Western blotting was performed after electrophoresis on Criterion SDS polyacrylamide gels (BioRad, Hercules, CA) and transfer to nitrocellulose membranes. Antibodies used were: rabbit anti-succinyllysine (PTM Biolabs), anti-malonyllysine (PTM Biolabs), anti-acyl-CoA oxidase-1 (ACOX1; Abcam), anti-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (EHHADH; Abcam), and anti-β-actin (Proteintech). After incubation with HRP-conjugated secondary antibodies (1:5000) blots were visualized with chemiluminescence. In some experiments the blots were scanned and subjected to densitometric analysis using ImageJ software.
Goetzman E.S., Bharathi S.S., Zhang Y., Zhao X.J., Dobrowolski S.F., Peasley K., Sims-Lucas S, & Monga S.P. (2020). Impaired mitochondrial medium-chain fatty acid oxidation drives periportal macrovesicular steatosis in sirtuin-5 knockout mice. Scientific Reports, 10, 18367.
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2

Mitochondrial Protein Immunoblotting

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Aliquots of total liver or heart mitochondrial protein were electrophoresed on Criterion SDS polyacrylamide gels (BioRad, Hercules, CA) and transferred to nitrocellulose membranes. Primary antibodies used for immunoblotting were: anti-TFPα (Abcam, 1:1000), TFPβ (Santa Cruz, 1:250), anti-SCHAD (Abcam, 1:2000), anti-acetyllysine (Cell Signaling, 1:1000), anti-succinyllysine (PTM Biolabs, 1:1000) and anti-heat shock protein-60 (Hsp60, Cell Signaling, 1:2000) as a mitochondrial marker for loading control. After incubation with HRP-conjugated secondary antibodies (1:5000) blots were visualized with chemiluminescence. The blots were scanned and subjected to densitometric analysis using ImageJ software, normalized to either Hsp60 or to Ponceau S membrane staining.
Zhang Y, & Goetzman E. (2021). The enzyme activity of mitochondrial trifunctional protein is not altered by lysine acetylation or lysine succinylation. PLoS ONE, 16(10), e0256619.
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3

Western Blot Analysis of Mitochondrial Proteins

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Western blotting was executed according to well-established procedures in our laboratory [43 (link), 83 (link), 46 (link), 65 (link), 44 (link), 35 (link)]. Equal amounts of mitochondrial or cytosolic protein per lane were electrophoresed on Criterion SDS-polyacrylamide gels (Bio-Rad) and transferred to polyvinylidene difluoride membranes (Millipore). After blocking, samples were probed with primary antibodies against cyclophilin D (CypD; AbCam, 1:12,000, 5 μg), SIRT3 (1:12,000, 5 μg), acetylated-lysine (1:1,000, 20 μg), LC3B (1:1,000, 20 μg), and Drp1 (Santa Cruz, 1:1,000, 20 μg). Proteins were visualized using enhanced chemiluminescence (GE Amersham) and densitometry performed using ImageJ. SYPRO Ruby staining (Invitrogen, Grand Island, NY) of the membrane was performed and visually inspected for consistency of protein loading [70 (link)]. All antibodies were purchased from Cell Signaling unless otherwise specified. Groups studied for western blotting were adult sham (n=3), adult I/R (n=5), MO OVX sham (n=4), and MO OVX I/R (n=6).
Garvin A.M., Aurigemma N.C., Hackenberger J.L, & Korzick D.H. (2017). Age and Ischemia Differentially Impact Mitochondrial Ultrastructure and Function in a Novel Model of Age-Associated Estrogen-Deficiency in the Female Rat Heart. Pflugers Archiv : European journal of physiology, 469(12), 1591-1602.
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4

Western Blot Analysis of Sirt2 and Other Proteins

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Tissue lysates in buffer containing 0.05% NP-40, 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl (pH 7.4), and 10 mM NAM with 1X EDTA-free protease inhibitors (Roche Life Sciences, Basel, Switzerland) were electrophoresed on Criterion SDS polyacrylamide gels (Bio-Rad, Hercules, CA, USA) and transferred to nitrocellulose membranes. The primary antibodies used were anti-Sirt2 (ab67299; Abcam), anti-GAPDH (G8795; Sigma-Aldrich, St. Louis, MO, USA), anti-c-MYC (Cat # 5605; Cell Signaling, Danvers, MA, USA), anti-Alpha tubulin (Cat # 66031-1-Ig, Proteintech, Rosemont, IL, USA), and anti-Lamin A/C (Cat # 10298-1-AP; Proteintech). After incubation with 1:10,000 Goat anti-Rabbit-HRP IgG (STAR208P; Bio-Rad) or Goat anti-Mouse-HRP IgG secondary antibody (STAR207P; Bio-Rad), the blots were visualized with Clarity Max ECL (BioRad), scanned, and in some cases subjected to densitometric analysis using ImageJ software.
Schmidt A.V., Monga S.P., Prochownik E.V, & Goetzman E.S. (2023). A Novel Transgenic Mouse Model Implicates Sirt2 as a Promoter of Hepatocellular Carcinoma. International Journal of Molecular Sciences, 24(16), 12618.
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