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Cat. No.: RBT1-60 (for 60U)

Cat. No.: RBT1-300 (for 300U)

Description

Butelase 1 is an asparagine ligase derived from Clitoria ternatea that specifically recognizes the Asn-His-Val amino acid sequence at the C-terminus of peptides. It catalyzes the formation of an Asn-Xaa peptide bond between the Asn residue of this sequence and any amino acid residue (Xaa) at the N-terminus of the same or another peptide. It is currently the most efficient peptide ligase available. Recombinant Butelase 1 is a high-purity enzyme preparation produced by heterologous expression after genetic engineering modification, with catalytic efficiency consistent with that of the wild-type Butelase 1. It features high specificity, broad substrate spectrum, simple recognition motif, and fast catalytic rate. Recombinant Butelase 1 efficiently catalyzes intramolecular cyclization and intermolecular ligation of peptides, and can be used for cyclizing biologically active peptides (such as antihypertensive peptides, antimicrobial peptides, analgesic peptides), linking peptides or proteins, in vivo and in vitro labeling of proteins or live cells, and conjugating peptides or proteins with functional molecules (such as nucleic acids, biotin, etc.).

Enzyme Activity

Using KB1-NHV peptide as the standard substrate, at a reaction pH of 6.0, the amount of enzyme required to catalyze the cyclization of 1 nmol of KB1-NHV within 1 minute is defined as one unit of enzyme activity (1 U).