Protein fusion tags are indispensible tools used to improve recombinant protein expression
yields, enable protein purification, and accelerate the characterization of protein structure …

In response to the rapidly growing field of proteomics, the use of recombinant proteins has
increased greatly in recent years. Recombinant hybrids containing a polypeptide fusion …

Inteins are auto-processing domains found in organisms from all domains of life. These
proteins carry out a process known as protein splicing, which is a multi-step biochemical …

Fok I is a type IIs restriction endonuclease comprised of a DNA recognition domain and a
catalytic domain. The structural similarity of the Fok I catalytic domain to the type II restriction …

A method is described to express and purify human DNA (cytosine-5) methyltransferase
(human DNMT1) using a protein splicing (intein) fusion partner in a baculovirus expression …

Affinity tags have become powerful tools from basic biological research to structural and
functional proteomics. They were widely used to facilitate the purification and detection of …

A novel protein purification system has been developed which enables purification of free
recombinant proteins in a single chromatographic step. The system utilizes a modified …

A split intein capable of protein trans-splicing is identified in a DnaE protein of the
cyanobacterium Synechocystis sp. strain PCC6803. The N-and C-terminal halves of DnaE …

▪ Abstract Protein splicing is a form of posttranslational processing that consists of the
excision of an intervening polypeptide sequence, the intein, from a protein, accompanied by …

Two cytotoxic proteins, bovine pancreatic ribonuclease A (RNase A), and a restriction
endonuclease from Haemophilus parainfluenzae (HpaI), were produced using a novel …