Cat#:EGC-098TS;Product Name:Endoproteinase Glu-C;Synonym:Endoproteinase,Endoproteinase Glu-C;Background:Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids.[1] For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins.;Description:Endoproteinase Glu-C is a serine proteinase which preferentially cleaves peptide bonds C-terminal to glutamic acid residues. It also cleaves at aspartic acid residues at a rate 100-300 times slower than at glutamic acid residues. ;Source:Bacillus subtilis;Molecular Characterization:29849 daltons;Concentration:100 - ng/μl;Storage:Store Endoproteinase Glu-C at -20°C. Optimal activity and stability for up to 12 months;Usage:For Lab Research Use Only;Components:GluC Reaction Buffer;Reaction Conditions:1X GluC Reaction Buffer Incubate at 37°C. 1X GluC Reaction Buffer: 50 mM Tris-HCl 0.5 mM Glu-Glu (pH 8 @ 25°C);References:Breddam, K. and Meldal, M. Substrate preference of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. Eur. J. Biochem.. 206;
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids.[1] For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins.
Description:
Endoproteinase Glu-C is a serine proteinase which preferentially cleaves peptide bonds C-terminal to glutamic acid residues. It also cleaves at aspartic acid residues at a rate 100-300 times slower than at glutamic acid residues.
Source:
Bacillus subtilis
Molecular Characterization:
29849 daltons
Concentration:
100 - ng/μl
Usage:
For Lab Research Use Only
Components:
GluC Reaction Buffer
Reaction Conditions:
1X GluC Reaction Buffer Incubate at 37°C. 1X GluC Reaction Buffer: 50 mM Tris-HCl 0.5 mM Glu-Glu (pH 8 @ 25°C)
Storage:
Store Endoproteinase Glu-C at -20°C. Optimal activity and stability for up to 12 months
References:
Breddam, K. and Meldal, M. Substrate preference of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. Eur. J. Biochem.. 206