This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide. Source: Recombinant protein corresponding to aa31-260 from Hypoderma lineatum Collagenase, fused to 10X His-Tag at N-terminal and Myc-Tag at C-terminal, expressed in E.coli. Molecular Weight: ~32.7kD Amino Acid Sequence: IINGYEAYTGLFPYQAGLDITLQDQRRVWCGGSLIDNKWILTAAHCVHDAVSVVVYLGSAVQYEGEAVVNSERIISHSMFNPDTYLNDVALIKIPHVEYTDNIQPIRLPSGEELNNKFENIWATVSGWGQSNTDTVILQYTYNLVIDNDRCAQEYPPGIIVESTICGDTSDGKSPCFGDSGGPFVLSDKNLLIGVVSFVSGAGCESGKPVGFSRVTSYMDWIQQNTGIIF 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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