Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). Source: Recombinant protein corresponding to aa1-194 from full length Clostridium botulinum ATP-dependent Clp Protease Proteolytic Subunit, fused to His-SUMO-Tag at N-terminal, expressed in E. coli. Molecular Weight: ~37.5kD Amino Acid Sequence: MSLVPVVVEQTNRGERSYDIYSRLLKDRIIMLSEEVNDTTASLIVAQLLFLEAEDPDKDIHLYINSPGGSITSGMAIYDTMQYIKPDVSTICVGMAASMGAFLLAAGAKGKRYALPNSEVMIHQPLGGFRGQATDIGIHAERILKMKKKLNTILSDRTGKPLEQVELDTERDHFLSAEEAKEYGLIDEVIDKKK 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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