Recombinant Lysobacter Enzymogenes Arg-C
Catalog Number : 450-54
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. Arg-C specifically cleaves at the carboxyl side of Arginine residues. Arg-C has a sulfhydryl requirement; it is activated by dithiothreitol, cysteine, or other sulfhydryl containing reagents. The presence of calcium ions is essential. The enzyme is inhibited by oxidizing agents and sulfhydryl reactants and by Co2+, Cu2+, Cd2+, and heavy metal ions. Recombinant Lysobacter Enzymogenes Arg-C is a 26.8 kDa protease consisting of 252 amino acid residues including a C-terminal His-Tag.
Hi-5 Insect cells
Above 98% as determined by SDS-PAGE Analysis.
The reaction is measured as an increase in absorbance at 253 nm resulting from the hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE).
GVGDIGSSD YCEKDIVCR VKPSAEFLS ASKSVARMV FTPKTGYTG YCSGTLLNN SNSPKRQLF WSAAHCIST QKVANTLQT YWLYDATGC DNDTLSDKA VTLTGGATL LHSHATRDT LLLELKSAP PSGAYYAGW NSSAIATKG TAIEGIHHP SGDLKKYSL GSVTALSST IDGKKPLTK VAWTTGVTE GGSSGSGLF TISSTSGYQ LRGGLYGGT SYCSAPSDP DYYSQLDGV WSSIKTYFS PHHHHHHHH
|Research Interest:||Immunology, Cancer|
|Protein Cross Reactivity:||NULL|