Product Name :
MMP-8 (catalytic domain) (human), (recombinant)

Sequence:

Purity:
≥90% (SDS-PAGE)

Molecular Weight:
20.3 kDa

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Additional Information :
| Activity Preincubation of MMP-8 catalytic domain at 13.6 nM with the broad-spectrum inhibitor GM6001 (Prod #BML-EI300) at 20nM for 1 hour completely inhibits enzymatic activity. | Alternative Name Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase-2 | Application Notes Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors. | Formulation Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol. | MW 20.3 kDa | Purity ≥90% (SDS-PAGE) | Purity Detail Purified by multi-step chromatography. | Source Produced in E. coli. Active Matrix Metalloproteinase-8 (MMP-8, neutrophil collagenase, collagenase-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-8 (Phe99-Gln269, NM_002424) with a C-terminal purification tag.{{2630904-45-7} MedChemExpress|{2630904-45-7} Protocol|{2630904-45-7} In stock|{2630904-45-7} manufacturer} This represents a naturally-occurring active form of MMP-8 which lacks the C-terminal hemopexin domain1.{{7196-71-6} medchemexpress|{7196-71-6} Purity & Documentation|{7196-71-6} In Vivo|{7196-71-6} custom synthesis} MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.PMID:31082121 | Specific Activity ≥2000 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. | UniProt ID P22894

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