Fusion proteins for identifying proteases, protease target...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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C435S023000, C435S024000, C435S007200, C435S007210, C435S069100, C435S069200, C435S069700, C536S023400, C536S023100, C536S023200

Reexamination Certificate

active

06884870

ABSTRACT:
The invention provides a fusion protein including a reporter polypeptide, a linker polypeptide comprising a protease cleavage site, and a repressor polypeptide. The repressor polypeptide represses the activity of the reporter polypeptide by conferring a specific localization in a cell that reduces activity of the reporter activity until the cleavage site is cleaved. A method is also provided for identifying a protease that recognizes a specific protease cleavage site. The invention further provides a method of identifying a compound that activates a protease.

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Sakai et al., Sterol-regulated Release of SREBP-2 from Cell Membranes Requires Two Sequential Cleavages, One Within a Transmembrane Segment, Jun. 1996, Cell, vol. 85, pp 1037-1046.*
Knight et al. Fluorimetric Assays of Protelytic Enzymes, Methods in Enzymology 248: 18-34, 1995.*
Sarubbi et al., “A high throughput assay for inhibitors of HIV-1 protease,”FEBS, 279(2):265-269 (1991).
Wearne, S. J., “Factor Xa cleavage of fusion proteins, Elimination of non-specific cleavage by reversible acylation,”FEBS, 263(1):23-26 (1990).

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