Staphylococcus Glu-C Recombinant eiwit

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Glu-C cleaves at the Carboxyl side of E (can also cleave D under certain conditions) . Recombinant Staphylococcus Glu-C is a 28.8 kDa protease consisting of 266 amino acid residues.

17368967

U5SV46

YP_008715574.1

Recombinant Proteins

E. coli

Room Temp

The lyophilized Staphylococcus Glu-C recombinant protein is stable for at least 2 years from date of receipt at -20˚ C. Reconstituted Staphylococcus Glu-C is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚ C. As with any protein, exposing Staphylococcus Glu-C recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.

Glutamyl endopeptidase precursor, serine proteinase SspA

Staphylococcus aureus subsp. aureus Z172

SAZ172_0989

Staphylococcus Glu-C

554643783

Lyophilized