Recombinant Glu-C, Lyophilized

Description

Glu-C protease, derived from Staphylococcus aureus V8 (S. aureus V8) and also known as V8 protease, is expressed in E. coli. This enzyme specifically hydrolyzes the peptide bonds at the carboxyl terminus of glutamic acid (Glu) or aspartic acid (Asp) residues. Its specificity is directly influenced by the components of the buffer. In NH₄HCO₃ buffer at pH 7.8 and CH₃COONH₄ buffer at pH 4.0, it recognizes and cleaves the peptide bonds at the carboxyl terminus of Glu. In phosphate buffer at pH 7.8, it recognizes and cleaves the peptide bonds at the carboxyl terminus of either Glu or Asp, and the hydrolysis rate for Glu is higher than that for Asp. The pH range for the enzyme's activity is 4.0-9.0. It can be used alone or in combination with other specific proteases for the enzymatic hydrolysis of protein solutions.

• Unit definition: One unit (U) is defined as the amount of enzyme required to catalyze the substrate (Z-Phe-Leu-Glu-4-pNA) to generate 1 μmol of p-nitroaniline (pNA) per minute under the conditions of 25 °C and pH 7.8.
• Storage solution (Before lyophilization)：50 mM Hepes，pH 7.8.

Product components