Cold-adapted protease enables quantitation of surface proteins in the absence of membrane trafficking | Zendy

Faraz Ahmad | Zendy; Sarah K. Coleman | Zendy; Kai Kaila | Zendy; Peter Blaesse | Zendy

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Cold-adapted protease enables quantitation of surface proteins in the absence of membrane trafficking

Author(s) -

Faraz Ahmad,

Sarah K. Coleman,

Kai Kaila,

Peter Blaesse

Publication year - 2011

Publication title -

biotechniques

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.617

H-Index - 131

eISSN - 1940-9818

pISSN - 0736-6205

DOI - 10.2144/000113651

Subject(s) - biotinylation , protease , trypsin , enzyme , cleavage (geology) , biochemistry , membrane , membrane protein , chemistry , biotin , biology , microbiology and biotechnology , chromatography , paleontology , fracture (geology)

We report here an improved method for analyzing protein surface expression utilizing a cold-adapted trypsin. Preservation of activity of the enzyme at 0-4°C permits modification of the protease method of surface analysis to temperatures at which trafficking of mammalian plasmalemmal proteins is blocked. This is an important advantage over established trypsin-cleavage protocols. Moreover, the method is less time-consuming than surface biotinylation.

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