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Endoproteinase Glu-C Online Inquiry

Cat#:EGC-098TS
Product Name:Endoproteinase Glu-C
Synonym: Endoproteinase,Endoproteinase Glu-C
Gene Introduction: 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

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