Chymotrypsin Protease, 70u, Mass Spectra Grade

Chymotrypsin is a serine endoprotease that specifically cleaves peptide bonds at the C-terminus of tyrosine (Tyr), phenylalanine (Phe), tryptophan (Trp), and leucine (Leu) residues. It also exhibits minor cleavage activity at the C-terminus of methionine (Met), alanine (Ala), aspartic acid (Asp), and glutamic acid (Glu). Residual trypsin activity is removed through TLCK inactivation and purification. The enzyme is activated and stabilized by Ca²⁺ ions.

Physical Form: Mass spectrometry-grade α-chymotrypsin protease is provided as a lyophilized powder.
Reconstitution: Reconstitute in 100 µL of 1 mM HCl containing 2 µM CaCl₂ before use.
Shelf Life: Stable for 12 months as lyophilized powder when stored at –20°C.
pH Range: Chymotrypsin exhibits optimal activity at pH 7.8.
Application: Chymotrypsin specifically hydrolyzes denatured proteins at Tyr (Y), Phe (F), Trp (W), and Leu (L) residues.

In-solution Digestion SOP:
Use chymotrypsin at a 1:50 (w/w) enzyme-to-protein ratio.
Perform digestion in 100 mM Tris-HCl buffer containing 10 mM CaCl₂ (pH 7.8) at 30°C for 2–12 hours.

Cleavage Sites: F, Y, W, L

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