HepG2 cells were collected at 48 hours after siRNA transfection mediated by SSPEI-SPIO nanoparticles. HepG2 cells were lysed in an ice-cold lysis buffer cocktail containing 1% Triton X-100 (Sigma-Aldrich Co.). Next, protein extracts were loaded into a 12.5% sodium dodecyl sulfate/polyacrylamide gel, electrophoresed, and transferred to a nitrocellulose membrane. After blocking with 5% non-fat dry milk, the membrane was washed in a Tris-buffered saline/Tween-20 mixture and co-incubated with a rabbit anti-hTERT primary mon-clonal antibody (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA) diluted at 1:500 in a 5% milk at 4°C overnight. The blot was then washed again in Tris-buffered saline/Tween-20 and incubated for 1 hour with horseradish peroxidase-conjugated donkey anti-rabbit IGg secondary antibody (Santa Cruz Biotechnology Inc.) diluted at 1:3000 in 5% milk. The blot signal was detected using Image Station 2000 MM System (Kodak, NY, USA) and analyzed with Kodak Molecular Imaging Software (Standard Edition V 5.0).
Image station 2000 mm system
Manufactured by Kodak
Sourced in United States
The Image Station 2000 MM System is a professional-grade lab equipment product designed for photographic image processing. It provides advanced features for scanning, digitizing, and managing photographic images. The system includes hardware and software components that enable high-quality image capture, storage, and manipulation.
Automatically generated - may contain errors
Lab products found in correlation
2 protocols using image station 2000 mm system
1
Western Blot Analysis of hTERT in HepG2 Cells
2
Detecting Viral Protein Interactions
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The cellular extracts of virus‐infected MDCK cells were prepared as described in previous section of immunoblotting. Before FlAsH‐EDT2 (Invitrogen) was added, the extracts were treated with or without β‐mercaptoethanol (final concentration 35.8 mm ; Merck) and boiled for 5 min. To test FlAsH‐EDT2 binding ability on the native NS1‐tc proteins, the extract was mixed with FlAsH‐EDT2 without any treatment. The labeling condition was set at 70 °C for 10 min with FlAsH‐EDT2 (final concentration 2 μm ) and then further incubated at room temperature for 1 h. Finally, the extract was analyzed by SDS/PAGE on a 12% polyacrylamide gel. The protein/FlAsH complexes were visualized on the gel with an appropriate filter for FlAsH fluorescence (excitation at 480 nm and emission at 535 nm) in Kodak image station 2000MM system. The same gel could be further analyzed for the total protein by Coomassie Blue staining or the specific NS1 with anti‐NS1 antiserum on the immunoblot.
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