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Clarity or clarity max western ecl blotting substrates

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Clarity or Clarity Max Western ECL Blotting Substrates are chemiluminescent detection reagents designed for western blotting analysis. They generate a luminescent signal in the presence of the horseradish peroxidase (HRP) enzyme, which can be detected using a compatible imaging system.

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Lab products found in correlation

Amersham hybond 0.45 pvdf membranes, by GE Healthcare (4 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (4 mentions) Anti rabbit secondary antibody, by Cell Signaling Technology (3 mentions) Cleaved caspase 3 antibody, by Cell Signaling Technology (3 mentions) Hrp conjugated anti β actin antibody, by Proteintech (3 mentions) Chemidoc touch system, by Bio-Rad (2 mentions) Iblot2 nc transfer stacks, by Thermo Fisher Scientific (2 mentions) Nupage bis tris protein gel, by Thermo Fisher Scientific (2 mentions) Protease inhibitor, by Roche (2 mentions) Precast sds polyacrylamide gel, by Bio-Rad (2 mentions) Anti p atr antibody, by Cell Signaling Technology (2 mentions) Anti atr antibody, by Cell Signaling Technology (2 mentions) P chk1 antibody, by Cell Signaling Technology (2 mentions) Beadbug homogenizer, by Benchmark Scientific (2 mentions) Penicillin streptomycin, by Thermo Fisher Scientific (1 mentions) Rpmi 1640 medium, by Thermo Fisher Scientific (1 mentions) Sds polyacrylamide gel, by Bio-Rad (1 mentions) Anti jnk antibody, by Cell Signaling Technology (1 mentions) Anti p p38 antibody, by Cell Signaling Technology (1 mentions) Anti p38 antibody, by Cell Signaling Technology (1 mentions)

7 protocols using clarity or clarity max western ecl blotting substrates

1

Protein Extraction and Western Blotting from SVG-A Cells

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SVG-A cells were lysed in a buffer containing 50 mM Tris-HCl (pH 7.5), 0.3 M NaCl, 0.5% Triton X-100, and protease inhibitors (1x, Roche) for 20 min on ice, with intense vortexing at the beginning and end of the incubation. Lysates were cleared by centrifugation at 18000xg for 15 min at 4°C before transferring the supernatant to new tubes. The protein content in the lysates and in the purified EV fractions was measured in the presence of 0.2% SDS, using Pierce BCA protein assay kit (Thermo Fisher Scientific) according to the manufacturer’s instructions. For each WB, 20 μg of lysates or 3 μg of EV pellets were loaded on 4%−12% NuPAGE Bis-Tris Protein Gels (Invitrogen) and ran under non-reducing conditions. Transfer was done using iBlot2 NC Transfer stacks (Invitrogen) prior to primary antibody incubation overnight at 4°C. Membranes were revealed by chemiluminescence using Clarity or Clarity Max Western ECL Blotting Substrates (Bio-Rad) and images were acquired using ChemiDoc Touch system (Bio-Rad).
Coulter M.E., Dorobantu C.M., Lodewijk G.A., Delalande F., Cianferani S., Ganesh V.S., Smith R.S., Lim E.T., Xu C.S., Pang S., Wong E.T., Lidov H.G., Calicchio M.L., Yang E., Gonzalez D.M., Schlaeger T.M., Mochida G.H., Hess H., Allen Lee W.C., Lehtinen M.K., Kirchhausen T., Haussler D., Jacobs F.M., Gaudin R, & Walsh C.A. (2018). The ESCRT-III Protein CHMP1A Mediates Secretion of Sonic Hedgehog on a Distinctive Subtype of Extracellular Vesicles. Cell reports, 24(4), 973-986.e8.
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2

Protein Extraction and Western Blotting from SVG-A Cells

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SVG-A cells were lysed in a buffer containing 50 mM Tris-HCl (pH 7.5), 0.3 M NaCl, 0.5% Triton X-100, and protease inhibitors (1x, Roche) for 20 min on ice, with intense vortexing at the beginning and end of the incubation. Lysates were cleared by centrifugation at 18000xg for 15 min at 4°C before transferring the supernatant to new tubes. The protein content in the lysates and in the purified EV fractions was measured in the presence of 0.2% SDS, using Pierce BCA protein assay kit (Thermo Fisher Scientific) according to the manufacturer’s instructions. For each WB, 20 μg of lysates or 3 μg of EV pellets were loaded on 4%−12% NuPAGE Bis-Tris Protein Gels (Invitrogen) and ran under non-reducing conditions. Transfer was done using iBlot2 NC Transfer stacks (Invitrogen) prior to primary antibody incubation overnight at 4°C. Membranes were revealed by chemiluminescence using Clarity or Clarity Max Western ECL Blotting Substrates (Bio-Rad) and images were acquired using ChemiDoc Touch system (Bio-Rad).
Coulter M.E., Dorobantu C.M., Lodewijk G.A., Delalande F., Cianferani S., Ganesh V.S., Smith R.S., Lim E.T., Xu C.S., Pang S., Wong E.T., Lidov H.G., Calicchio M.L., Yang E., Gonzalez D.M., Schlaeger T.M., Mochida G.H., Hess H., Allen Lee W.C., Lehtinen M.K., Kirchhausen T., Haussler D., Jacobs F.M., Gaudin R, & Walsh C.A. (2018). The ESCRT-III Protein CHMP1A Mediates Secretion of Sonic Hedgehog on a Distinctive Subtype of Extracellular Vesicles. Cell reports, 24(4), 973-986.e8.
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3

Western Blot Analysis of Cell Signaling

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Tumor tissues were homogenized using a BeadBug Homogenizer (Benchmark Scientific, Sayreville, NJ). Protein lysates were prepared with lysis buffer (1% Triton X-100, 0.05% SDS, 100 mM Na2HPO4, and 150 mM NaCl). Protein lysate was electrophoresed on a 4–20% pre-cast SDS-polyacrylamide gel (Bio-Rad, Hercules, CA) and transferred onto Amersham Hybond 0.45 PVDF membranes (GE Healthcare, Chicago, IL). After blocking with 5% non-fat milk in PBS-0.05% Tween 20, the membranes were incubated with primary antibodies at 4°C overnight, and then secondary antibodies for 1 h at room temperature. Antibodies include anti-p-ATR antibody (#2853, Cell Signaling Technology), anti-ATR antibody (#13934, Cell Signaling Technology), p-CHK1 antibody (#2348, Cell Signaling Technology, Danvers, MA), cleaved-caspase-3 antibody (#9664, Cell Signaling Technology), HRP-conjugated anti-β-actin antibody (#HRP-6008, ProteinTech), anti-rabbit secondary antibody (#7074, Cell Signaling Technology). The blots were developed using Clarity or Clarity Max Western ECL Blotting Substrates (Bio-Rad).
Harold J., Bellone S., Manavella D.D., Mutlu L., McNamara B., Hartwich T.M., Zipponi M., Yang-Hartwich Y., Demirkiran C., Verzosa S.M., Choi J., Dong W., Buza N., Hui P., Altwerger G., Huang G.S., Andikyan V., Clark M., Ratner E., Azodi M., Schwartz P.E, & Santin A.D. (2022). Elimusertib (BAY1895344), a Novel ATR Inhibitor, Demonstrates in vivo Activity in ATRX Mutated Models of Uterine Leiomyosarcoma. Gynecologic oncology, 168, 157-165.
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4

Elimusertib Effects on DNA Damage Response

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Cells were cultured in RPMI 1640 medium (Life Technologies, Grand Island, NY) containing 10% fetal bovine serum (Seradigm, Radnor, PA) and penicillin/streptomycin (Life Technologies) at 37°C and 5% CO2. They were treated with a medium containing elimusertib (0.3 μM or 3 μM) or DMSO solvent (0.03%) which functioned as the untreated control. At the desired time points, cells were trypsinized and collected for preparing protein lysates. Protein lysates were prepared with lysis buffer (1% Triton X-100, 0.05% SDS, 100 mM Na2HPO4, and 150 mM NaCl) and then electrophoresed on a 4-20% pre-cast SDS-polyacrylamide gel (Bio-Rad) and transferred onto Amersham Hybond 0.45 PVDF membranes (GE Healthcare, Chicago, IL). After blocking with 5% non-fat milk in PBS-0.05% Tween 20, the membranes were incubated with primary antibodies at 4°C overnight, and then secondary antibodies for 1 h at room temperature. Antibodies include anti-p-ATR antibody (#2853, Cell Signaling Technology), anti-ATR antibody (#13934, Cell Signaling Technology), p-CHK1 antibody (#2348, Cell Signaling Technology), cleaved-caspase-3 antibody (#9664, Cell Signaling Technology), HRP-conjugated anti-β-actin antibody (#HRP-6008, ProteinTech), anti-rabbit secondary antibody (#7074, Cell Signaling Technology). The blots were developed using Clarity or Clarity Max Western ECL Blotting Substrates (Bio-Rad).
Manavella D.D., McNamara B., Harold J., Bellone S., Philipp Hartwich T.M., Yang-Hartwich Y., Mutlu L., Zipponi M., Demirkiran C., Verzosa M.S., Altwerger G., Ratner E., Huang G.S., Clark M., Andikyan V., Azodi M., Schwartz P.E., Dottino P.R., Choi J., Alexandrov L.B., Buza N., Hui P, & Santin A.D. (2022). Ovarian and uterine carcinosarcomas are sensitive in vitro and in vivo to Elimusertib, a novel ataxia-telangiectasia and Rad3-related (ATR) kinase inhibitor. Gynecologic oncology, 169, 98-105.
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5

Protein Expression Analysis in Tumor Tissues

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Tumor tissues were homogenized using a BeadBug Homogenizer (Benchmark Scientific). Protein lysates were prepared with lysis buffer (1% Triton X-100, 0.05% SDS, 100 mM Na2HPO4, and 150 mM NaCl). Protein lysate was electrophoresed on a 4–20% pre-cast SDS-polyacrylamide gel (Bio-Rad, Hercules, CA) and transferred onto Amersham Hybond 0.45 PVDF membranes (GE Healthcare, Chicago, IL). After blocking with 5% non-fat milk in PBS-0.05% Tween 20, the membranes were incubated with primary antibodies at 4°C overnight, and then secondary antibodies for 1h at room temperature. Antibodies include anti-p-MAP2K4 antibody (#9156, Cell Signaling Technology), anti-MAP2K4 antibody (#9152, Cell Signaling Technology), anti-p-JNK antibody (#9255, Cell Signaling Technology), anti-JNK antibody (#9252, Cell Signaling Technology), anti-p-p38 antibody (#9211, Cell Signaling Technology), anti-p38 antibody (#8690, Cell Signaling Technology), anti-PARP-1 antibody (#9532, Cell Signaling Technology), HRP-conjugated anti-β-actin antibody (#HRP-6008, ProteinTech), cleaved-caspase-3 antibody (#9664, Cell Signaling Technology), anti-rabbit secondary antibody (#7074, Cell Signaling Technology). The blots were developed using Clarity or Clarity Max Western ECL Blotting Substrates (Bio-Rad).
Stead D, & Park S.F. (2000). Roles of Fe Superoxide Dismutase and Catalase in Resistance of Campylobacter coli to Freeze-Thaw Stress. Applied and Environmental Microbiology, 66(7), 3110-3112.
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6

Protein Extraction and Western Blotting

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Proteins were extracted from tissues and cells using a high-salt buffer solution with Hepes 25 mM, EDTA 0.2 M (pH 8), MgCl2 1.5 mM, NaCl 0.4 M, Nonidet-P40 1% supplemented with NaF 1 mM, Na3VO4 1 mM, phenylmethylsulfonyl fluoride 1 mM, and complete protease inhibitor cocktail (Roche, Bâle, Switzerland). A total of 40 μg of total proteins were loaded on 4% to 12% Invitrogen NuPAGE Bis-Tris protein precast polyacrylamide gels and transferred onto Trans-Blot Turb Mini PVDF membranes. Membranes were incubated overnight at 4°C with primary antibodies either with 5% non-fat dry milk or BSA. Primary antibody detection was performed using peroxidase-conjugated anti-rabbit or anti-mouse antibodies (Abliance, Compiègne, France) and Clarity or Clarity Max Western ECL Blotting Substrates (Bio-Rad). Antibodies used for western blots are listed in SI Appendix S3 Table.
Bousset L., Septier A., Bunay J., Voisin A., Guiton R., Damon-Soubeyrant C., Renaud Y., De Haze A., Sapin V., Fogli A., Rambur A., De Joussineau C., Kocer A., Trousson A., Henry-Berger J., Höring M., Liebisch G., Matysik S., Lobaccaro J.M., Morel L, & Baron S. (2020). Absence of nuclear receptors LXRs impairs immune response to androgen deprivation and leads to prostate neoplasia. PLoS Biology, 18(12), e3000948.
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7

Western Blot Analysis Protocol

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Cell lysates were prepared with cell lysis buffer (1% Triton X-100, 0.05% SDS, 100 mM Na2HPO4, and 150 mM NaCl). Protein lysate was electrophoresed on a 12% SDS-polyacrylamide gel and transferred onto Amersham Hybond 0.45 PVDF membranes (GE Healthcare, Chicago, IL). After blocking with 5% non-fat milk in PBS-0.05% Tween 20, the membranes were incubated with primary antibodies at 4°C overnight, and then secondary antibodies for 1 h at room temperature. The blots were developed using Clarity or Clarity Max Western ECL Blotting Substrates (Bio-Rad).
Bi F., Jiang Z., Park W., Hartwich T.M., Ge Z., Chong K.Y., Yang K., Morrison M.J., Kim D., Kim J., Zhang W., Kril L.M., Watt D.S., Liu C, & Yang-Hartwich Y. (2021). A Benzenesulfonamide-based Mitochondrial Uncoupler Induces Endoplasmic Reticulum Stress and Immunogenic Cell Death in Epithelial Ovarian Cancer. Molecular cancer therapeutics.
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