CinderBio products
Krakatoa cuts at E, L, and F residues preferentially. Using brief one-step HTA-Protease reaction protocols significantly increase proteome and protein sequence coverage with datasets orthogonal to trypsin and have shown a bias for ribonucleoproteins, histones, mitochondrial, and membrane proteins.
Vesuvius cuts at E, L, and F residues preferentially. Using brief one-step HTA-Protease reaction protocols significantly increase proteome and protein sequence coverage with datasets orthogonal to trypsin and have shown a bias for ribonucleoproteins, histones, mitochondrial, and membrane proteins.
How Vesuvius and Krakatoa are similar and different
CinderBio’s HTA-Proteases Vesuvius and Krakatoa are both classified as ‘thermopsin’ proteases and derived from different species of acid and heat loving Archaea of the same genus. Both enzymes show a cleavage preference for E, L, and F amino acids but result in significantly different peptide and protein identifications. Digestion of K562 cell extracts reveals only 11% of peptide and 63% of protein identifications are common to both enzymes. The mechanism(s) for this selectivity are not yet fully understood. Vesuvius and Krakatoa are compatible with simultaneous co-digestion and sequential digestion of the same sample as useful.
Bringing the Third Domain of Life to Biotechnology
Both Krakatoa and Vesuvius proteases are shipped ready-to-use and have extremely high activities and rapid digestion kinetics in heated acidic conditions that obviate the use of chaotropes (80° C, pH 3.0). Both HTA-Proteases show a bias for membrane and nucleoproteins. HTA-Proteases function in acetic, nitric, phosphoric, citric, formic, and peracetic acids at reaction pH of 3.0. They are compatible with all tested detergents and surfactants, show no autolysis, and are quenched by refrigeration (4° C). HTA-Proteases are very unlike typical proteomics enzymes like trypsin and should be used and treated accordingly.
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