rTrypsin/rLys C Complex Protease, 15000u/25u, Mass Spectra Grade

rTrypsin 3.0 and rLys-C Proteases are recombinant metalloproteases. rTrypsin specifically and ultra-rapidly cleaves the C-terminal peptide bonds of arginine (R) and lysine (K), while rLys-C specifically and rapidly cleaves the C-terminal peptide bonds of lysine (K). Because trypsin does not digest arginine and lysine at the same rate, many lysine residues can remain uncleaved. Additionally, lysine residues with post-translational modifications (PTMs) or those immediately followed by strongly hydrophobic amino acids (e.g., proline) may also resist cleavage. The rTrypsin/rLys-C combination protease is suitable for processing complex protein samples that are difficult to digest.

Physical Form: Lyophilized powder containing 67 µg trehalose.
Reconstitution: Dissolve in 40 µL of 50 mM acetic acid to obtain a concentration of 0.5 µg/µL.
Shelf Life: 24 months when stored at –20°C.
pH Range: The combination protease exhibits optimal activity at pH 7–9.

Digestion Protocol:

Recommended digestion buffer: 20 mM Tris, 50 mM ammonium bicarbonate (ABC), or HEPES buffer; pH 7–9.

For denatured protein samples: Use the enzyme at a 1:50 (w/w) enzyme-to-protein ratio. Maintain the protein concentration at 0.5 µg/µL and incubate at 37°C in a dry bath for 30 minutes.

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