Enzo BML-SE180-0010 MMP-1 (catalytic domain) (human), (recombinant) (10 µg)

Preincubation of MMP-1 catalytic domain at 0.7 nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 20nM for 1 hour completely inhibits enzymatic activity.

Matrix metalloproteinase 1, Interstitial collagenase, Fibroblast collagenase

Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.

Liquid. In 50mM TRIS, pH 7.5, containing 5mM calcium chloride, 300mM sodium chloride, 20µM zinc chloride, 0.5% Brij-35, and 30% glycerol.

NM_002421 (RefSeq)

~19.9 kDa

≥95% (SDS-PAGE)

Purified by multi-step chromatography.

Produced in E. coli. Active Matrix Metalloproteinase-1 (MMP-1, interstitial collagenase, fibroblast collagenase) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-1 (Phe¹⁰⁰-Gln²⁶⁸) with a C-terminal purification tag.

≥5000 pmol/min/µg at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate.

P03956

The enzyme is stable on ice for at least several hours. However, it is recommended that thawing and dilution of the enzyme be done within as short a time as possible before start of the assay. Note: When stored under the recommended conditions, this enzyme is stable at the concentration supplied, in its current storage buffer. Procedures such as dilution of the enzyme followed by refreezing could lead to loss of activity.

Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.

-80°C

Dry Ice