The present product is a recombinant enzyme - inorganic pyrophosphatase of Thermococcus litoralis. The enzyme has a molecular mass of ~21 kDa and catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. The enzyme is active in a wide temperature range and is thermostable.

This product is a recombinant enzyme - alkaline phosphatase of the gram-negative bacterium Vibrio splendidus. Application • Cloning of restriction fragments. • mRNA synthesis.

The enzyme exhibits high specific activity against double-stranded DNA, while single-stranded DNA or RNA remain intact under standard conditions.

RNase A is an enzyme isolated from bovine pancreas. The enzyme is used to remove RNA in the isolation of genomic and plasmid DNA.
RNase A does not destroy DNA.

Recombinant DNA ligase of bacteriophage T4. T4 DNA ligase crosslinks both cohesive and blunt ends to form a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl ends in double-stranded DNA or RNA fragments. The enzyme also repairs single-strand breaks in double-stranded DNA.

Recombinant version of the catalytic domain of the nuclear inclusion protein of the Tobacco Etch Virus. TEV protease cleaves proteins at a specific site of seven amino acid residues of the following composition: Glu-Asn-Leu-Tyr-Phe-Glu-X (ENLYFQ-X).

An enzyme derived from the fungus Tritirachium album and produced by expression in the yeast Pichia pastoris. Proteinase K has broad cleavage specificity, cleaves many proteins, and retains its stability in the presence of detergents and urea.