A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective. Source: Recombinant protein corresponding to aa700-910 from mouse Mug1, fused to His-Tag at N-terminal, expressed in E. coli. Molecular Weight: ~27kD Amino Acid Sequence: TPEISWSLRTTLSKRPEEPPRKDPSSNDPLTETIRKYFPETWVWDIVTVNSTGLAEVEMTVPDTITEWKAGALCLSNDTGLGLSSVVPLQAFKPFFVEVSLPYSVVRGEAFMLKATVMNYLPTSMQMSVQLEASPDFTAVPVGDDQDSYCLSANGRHTSSWLVTPKSLGNVNFSVSAEAQQSSEPCGSEVATVPETGRKDTVVKVLIVEPE Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.
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