Protease Substrates Screening Service

Product Description

Phage display peptide libraries that display random ***0 mer peptides have been widely used to determine protease substrate [sequence] specificity for a large number of enzymes and semi-purified cell extracts. This technique has been playing a critical role in designing inhibitors and activators of proteases. 

In comparison with phage display peptide libraries used in other fields, phage display peptide libraries used to identify the preferred substrate sequences of a protease usually express a fusion tag at the N-terminus of the peptide sequences, while, like in regular phage display peptide libraries, the minor coat viral protein pIII is located at the C-terminus of the peptide sequences. The N-terminal fusion tag is intended to bind the phage particles to a solid support. Scientists from Creative Biolabs have designed and built up a unique tag, HiAffi-tag, which is derived from Protein G, thus has strong binding affinity to most IgG coated on a solid surface. In contrast to His Tag and Strepavidin Binding Motifs used in such libraries, HiAffi-tag enables the best capture of the phage particles to the solid support and the least steric hindrance for proteolysis of the substrate peptides.