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Advantages of Near-Infrared In-Gel Westerns

Two-fold serial dilutions of purified Transferrin were separated by electrophoresis on duplicate gels.

Figure 1. Sensitivity of Odyssey infrared In-Gel Westerns is equal to or better than chemiluminescence. Beginning with 10 ng/lane (far left), two-fold serial dilutions of purified Transferrin were separated by electrophoresis on duplicate gels. In-Gel Westerns were detected with infrared fluorescence (top) and chemiluminescence on film (bottom). Odyssey detection outperformed chemiluminescence.

  • Useful for difficult-to-transfer proteins1
    • Large, hydrophobic, or post-translationally-modified proteins, such as glycoproteins, receptors, or cell membrane proteins that do not transfer well
  • Multiplexed, two-color detection of two different protein targets within the same gel
  • Clearer, sharper bands than with in-gel chemiluminescent protocols (Fig. 1)
  • Nanogram to picogram detection sensitivity (Fig. 2)
  • Clean images with minimal background banding
  • In-Gel Westerns can be imaged with the Odyssey® CLx or Classic Imager
In-Gel detection of Cytochrome P450 3A4 (CYP3A4).

Figure 2. In-Gel detection of Cytochrome P450 3A4 (CYP3A4). Fixed gel was probed with anti-CYP3A4 primary antibody and IRDye® 800 secondary antibody. The limit of detection is approximately 3 ng. Reprinted with permission from Theisen, M. J. and Chiu, M. L. LI-COR Biosciences (2004)


1. Theisen, M. J. and Chiu, M. L. In-gel immunochemical detection of proteins that transfer poorly to membranes.



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