Affinity-Removable Recombinant Trypsin

Description

Affinity-Removable Recombinant Trypsin is a recombinant trypsin containing a C-terminal polyhistidine affinity tag and produced in Pichia pastoris. It combines proteolytic activity with a built-in affinity handle for immobilization or selective removal using Ni-NTA or other immobilized metal affinity chromatography (IMAC) matrices.

Trypsin preferentially cleaves peptide bonds on the C-terminal side of lysine and arginine residues. The C-terminal His tag enables removal of the protease after protein processing and reversible immobilization on metal-affinity supports—workflows that can be difficult with conventional untagged trypsin.

Key Features

• Recombinant production in Pichia pastoris
• C-terminal His tag provides a convenient affinity handle
• Affinity-removable following protein digestion or processing
• Compatible with Ni-NTA and other IMAC matrices
• Suitable for soluble and immobilized proteolysis workflows
• High purity demonstrated by SEC-HPLC

Applications

• Recombinant protein processing
• Controlled proteolysis
• Affinity-removable protease workflows
• Peptide mapping method development
• Protease immobilization studies

DOCUMENTS

Protocol

SDS