Staphylococcus aureus V-8 Protease

Staphylococcus aureus V-8 protease is an enzyme that specifically cleaves the COOH-terminal peptide bond of glutamic acid and aspartic acid. It has optimal activity at pH 4.0 and 7.8, and its specificity is restricted to the glutamic acid site in the presence of ammonium. The enzyme can be inhibited by diisopropylfluorophosphate and certain monovalent anions, and activity is typically assessed by casein digestion assays.

66676-43-5

66676-43-5; 620-751-3; EC 3.4.21.19; SplB serine protease; Endoproteinase Glu-C; Glu-C protease; Staphylococcus V8 serine endopeptidase; Glutamyl endopeptidase, V8 protease

27 kDa

Lyophilized powder

Store at 2-8°C for long term storage.

Staphylococcus aureus V-8 protease is an endonuclease that specifically cleaves glutamic acid residues in proteins and is widely used in proteomics research and protein sequence analysis. It helps researchers conduct protein structure and functions research, fragmentation, separation and purification processes by specifically hydrolyzing target sites.