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Synthetic peptide corresponding to residues close to SH3 domain of human Lyn
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMab® patents
Our Abpromise guarantee covers the use of ab32398 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/2000. Detects a band of approximately 56 kDa (predicted molecular weight: 53 kDa).|
Lane 1: Wild-type HAP1 cell lysate (20 µg)
Lane 2: Lyn knockout HAP1 cell lysate (20 µg)
Lane 3: Ramos cell lysate (20 µg)
Lane 4: A431 cell lysate (20 µg)
Lanes 1 - 4: Merged signal (red and green). Green - ab32398 observed at 60 kDa. Red - loading control, ab8245, observed at 37 kDa.
ab32398 was shown to specifically react with Lyn when Lyn knockout samples were used. Wild-type and Lyn knockout samples were subjected to SDS-PAGE. ab32398 and ab8245 (loading control to GAPDH) were diluted at 1/2000 and 1/10 000 respectively and incubated overnight at 4°C. Blots were developed with Goat anti-Rabbit IgG H&L (IRDye® 800CW) preadsorbed ab216773 and Goat anti-Mouse IgG H&L (IRDye® 680RD) preadsorbed ab216776 secondary antibodies at 1/10 000 dilution for 1 h at room temperature before imaging.
Lanes 1 - 3: Merged signal (red and green). Green - ab32398 observed at 60 kDa. Red - loading control, ab8245, observed at 37 kDa.
This blot was produced using a 4-12% Bis-tris gel under the MOPS buffer system. The gel was run at 200V for 50 minutes before being transferred onto a Nitrocellulose membrane at 30V for 70 minutes. The membrane was then blocked for an hour using Licor blocking buffer before being incubated with ab32398 and ab8245 (loading control) overnight at 4°C. Antibody binding was detected using Goat anti-Rabbit IgG H&L (IRDye® 800CW) preabsorbed (ab216773) and Goat anti-Mouse IgG H&L (IRDye® 680RD) preabsorbed (ab216776) at a 1:10000 dilution for 1hr at room temperature and then imaged.
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