Native Staphylococcus aureus Endoproteinase GluC

inquiry

Cat No.

NATZ-137

Description

This enzyme is isolated from Staphylococcus aureus V8 and specifically cleaves at the carboxyl side of glutamic acid residues. It cleaves peptide bonds at the carboxyl side of both glutamic acid and aspartic acid in phosphate buffer systems, and at the carboxyl side of glutamic acid in ammonium buffer systems. Due to its high substrate specificity, it is used for peptide mapping in various protein sequencing analyses.
1. Cleavage Exclusively at the Carboxyl Terminus of Glutamic Acid
Digest at 30–37°C for 2–24 hours in either 0.01–0.1 mol/L ammonium bicarbonate (pH 7.8) or 0.01–0.1 mol/L ammonium acetate (pH 4.0), with an enzyme-to-substrate molar ratio of 1:30–100.
2. Simultaneous Cleavage at the Carboxyl Terminus of Aspartic Acid
Digest under the same conditions as above in 0.01–0.1 mol/L phosphate buffer (pH 7.8).

Source

Staphylococcus aureus V8

Applications

Specifically cleaves at the carboxyl side of glutamic acid residues. Peptide mapping for sequence analysis of various proteins.

Form

White crystals or crystalline powder

Activity

20 units/mg or higher

CAS_No

66676-43-5

Molecular Weight

Approximately 27,000

Unit Definition

One unit is defined as the amount of enzyme that produces 1 μmol of 4-nitroaniline from the substrate 2-Phe-Leu-Glu-4-NA per minute at pH 7.8 and 25°C.

Optimum pH

Proteolytic activity is detectable across the pH range of 3.5–9.5, with maximum activity observed at pH 4.0 and pH 7.8 (using hemoglobin as the substrate).

Synonyms

Protease V8

First Name:

Last Name:

Email *

Phone Number:

Company/Institution:

Country or Region:

Quantity:

Services & Products of Interested

Project Description:

For research and industrial use only. Not intended for personal medicinal use. Certain food-grade products are suitable for formulation development in food and related applications.

Products

Online Inquiry