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Cell extracts for Histidine-Tagged (His-Tag) protein contain a number of endogenous proteases, that are capable of modifying the proteins present in the extract/lysate.
The need for protease inhibitors arises to protect the proteins from damage caused by these proteases released during the cellular lysis.
Also, to improve the yield of native proteins, use of protease inhibitor cocktail along with phosphatase and other inhibitors is recommended during the extraction process.
Our Histidine-Tagged (His-Tag) protease inhibitor cocktail contains optimized concentration of protease inhibitors: AEBSF (4-[2-Aminoethyl] benzenesulfonyl fluoride hydrochloride), Bestatin, Pepstatin A, E-64 (N-[trans-Epoxysuccinyl]-L-leucine 4-guanidinobutylamide), Phosphoramidon protease inhibitors and other proprietary component(s) for broad spectrum inhibition of proteases that target serine proteases (e.g., trypsin, chymotrypsin, plasmin, kallikrein, and thrombin), cysteine proteases (e.g., calpain, papain, cathepsin B, and cathepsin L), aminopeptidases (e.g., leucine aminopeptidase and alanyl aminopeptidase, acid proteases (e.g., pepsin, rennin, and cathepsin D, and many microbial aspartic proteases), and membrane metallo-endopeptidase (e.g., thermolysin and collagenase), etc.
Our Histidine-Tagged (His-Tag) protease inhibitor cocktail preserves proteins from degradation by proteases and can be used with the lysis buffer for His-Tag protein extractions or lysate.
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