66676-43-5

Basic information

• Product Name: EC 3.4.21.19
• Synonyms: EC 3.4.21.19;ENDOPROTEINASE GLU-C;ENDOPROTEINASE GLU-C, STAPHYLOCOCCUS AUREUS;STAPHYLOCOCCAL SERINE PROTEASE PROTEASE V8;STAPHYLOCOCCAL SERINE PROTEINASE;PROTEASE V8;PROTEASE, S AUREUS;PROTEASE TYPE XVII-B
• CAS NO: 66676-43-5
• Molecular Formula: NULL
• Molecular Weight: 0
• EINECS: 232-642-4
• Product Categories: enzyme
• Mol File: 66676-43-5.mol
• Article Data: 0

Chemical Properties

• Appearance: light brown/lyophilized powder
• Storage Temp.: −20°C
• Water Solubility: Soluble in water
• CAS DataBase Reference: EC 3.4.21.19(CAS DataBase Reference)
• NIST Chemistry Reference: EC 3.4.21.19(66676-43-5)
• EPA Substance Registry System: EC 3.4.21.19(66676-43-5)

Safety Data

• Hazard Codes: Xn
• Statements: 36/37/38-42/43
• Safety Statements: 22-24-26-36/37-45
• WGK Germany: 3
• RTECS: TW0175000
• F: 10
• Hazardous Substances Data: 66676-43-5(Hazardous Substances Data)

Usage

Uses

Different sources of media describe the Uses of 66676-43-5 differently. You can refer to the following data:
1. Endoproteinase Glu-C from Staphylococcus aureus strain V8 is a serine protease used for selective cleavage of proteins for amino acid sequence determination or peptide mapping . Product P2922 has been used to linearize cyclic peptides in C. ternatea leaf extract.
2. Endoproteinase Glu-C from Staphylococcus aureus V8 has been used for:obtaining proteolytic cleavage fragments of the S-layer protein (from Bacillus stearothermophilus ATCC 12980) to perform affinity studies.the enzymatic cleavage of native VSTx-3 (voltage sensor toxin 3) peptide for its sequence determination. limited proteolysis of recombinant purified PimA (phosphatidylinositol mannosyltransferase). the digestion of glycosylated hemoglobin for isotope dilution liquid chromatography-tandem mass spectrometry analysis.

Biochem/physiol Actions

Staphylococcus strain V8 protease specifically cleaves peptide bonds on the carboxyl side of aspartic and glutamic acid residues when used in phosphate buffer. When used in ammonium bicarbonate buffer or ammonium acetate buffer cleavage is restricted to the carboxyl side of glutamic acid residues only. The enzyme exhibits maximal activity from pH 4.0 to 7.8. If hemoglobin is used as the substrate, maximal activity is at pH 4.0. The maximal activity is at pH of 7.8 when casein is the substrate.