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Genentech's Study on the Peroxisomal Targeting Signal in Firefly Luciferase Reveals New Insights



Genentech has successfully leveraged the Firefly Luciferase Lysis Buffer 5X from Signosis for their groundbreaking study on the peroxisomal targeting signal in firefly luciferase. This study has shown that the COOH-terminal three amino acids of the protein, specifically serine-lysine-leucine, serve as the peroxisomal targeting signal.


This breakthrough discovery has significant implications for the field of molecular biology, as it provides a better understanding of how peroxisomal targeting occurs in cells. It also has important practical applications, as it can help in the development of targeted drug delivery systems.


Signosis' Firefly Luciferase Lysis Buffer 5X was critical to the success of this study, as it allowed for efficient lysis of cells and extraction of firefly luciferase. This enabled the researchers at Genentech to perform accurate and precise measurements of luciferase activity, leading to the discovery of the peroxisomal targeting signal.


Overall, this study demonstrates the importance of high quality and multiplex research tools, such as the Firefly Luciferase Lysis Buffer 5X from Signosis, in advancing scientific knowledge and discovery.




Antibodies directed against the peroxisomal targeting signal of firefly luciferase recognize multiple mammalian peroxisomal proteins (Open Access)

Gould, S.J., Krisans, S., Keller, G.-A., Subramani, S.

Department of Biology, Bonner Hall, University of California, San Diego, CA 92093, United States

San Diego State University, Department of Biology, San Diego, CA 92182, United States

Genentech, 460 San Bruno Blvd., South San Francisco, CA 94080, United States


Abstract

We have previously shown that the peroxisomal targeting signal in firefly luciferase consists of the COOH-terminal three amino acids of the protein, serine-lysine-leucine (Gould, S. J., G.-A. Keller, N. Hosken, J. Wilkinson, and S. Subramani, 1989. J. Cell Biol. 108:1657-1664). Antibodies were raised against a synthetic peptide that contained this tripeptide at its COOH terminus. Immunofluorescence and immunocryoelectron microscopy revealed that the anti-peptide antibodies specifically detected peroxisomes in mammalian cells. Further characterization revealed that the antibodies were primarily directed against the COOH-terminal three amino acids of the peptide. In Western blot experiments, the antibodies recognized 15-20 rat liver peroxisomal proteins, but reacted with only a few proteins from other subcellular compartments. These results provide independent immunological evidence that the peroxisomal targeting signal identified in firefly luciferase is present in many peroxisomal proteins.



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