Glutamylendopeptidase - Endoproteinase Glu-C.
Description
Glutamylendopeptidase (Endoproteinase Glu-C, EC 3.4.21.19) from Bacillus intermedius (recombinant producer in Bacillus subtilis), selectively hydrolyzes peptides bond formed by carboxyl moiety of glutamic acid. The Endoproteinase Glu-C specifically cleaves peptide bonds on the carboxyl side of aspartic and glutamic acid residues. M.W. approx. 24500.
 
Two grades of purity are available: P1.1. Single-step affinity chromatography Electrophoretic purity 99%, contains 0.1% of non-specific activity of alkaline protease. P1.2. Two-step affinity/FPLC chromatography Electrophoretic purity - 100% (contamination less than 0.01%). No concomitant protease activity.
Unit definition

One unit hydrolyzes 1.0 mM of Z-Glu-pNA (carbobenzoxy-glutamyl-para-nitroanilide) per min at pH 7.2 at 37°C.

Storage
Store below 0°C.
Applications
used for selective cleavage of proteins for amino acid sequence determination or peptide mapping.

Quality control

alkaline protease activity.

References

1. Drapeau, G.R. (1977) Meth. Enzymol. 47, 189. 2. Cleveland, D.W. et al. (1977) J. Biol. Chem. 252, 1102. 3. Leshchinskaya, I.B. et al. (1997) FEBS Lett. 404, 241-244.

Catalog #
P1

P1

P2

P2

 

Pack size

10 mg

100 mg

10 mg

100 mg

 

 

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