MMP8 - catalytic domain

Description
MW = 17.6 kDa calculated. Recombinant Matrix Metalloproteinase-8 (MMP-8, Collagenase-2, Neutrophil collagenase) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-8 (residues 105-262, UniProtKB accession P22894).

       110        120        130        140
    NPKWER TNLTYRIRNY TPQLSEAEVE RAIKDAFELW
       150        160        170        180 
SVASPLIFTR ISQGEADINI AFYQRDHGDN SPFDGPNGIL 
       190        200        210        220
AHAFQPGQGI GGDAHFDAEE TWTNTSANYN LFLVAAHEFG 
       230        240        250        260
HSLGLAHSSD PGALMYPNYA FRETSNYSLP QDDIDGIQAI

YG

Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 14.4 and 18.4 kDa.

Supplied as
0.2 mg/mL solution in Tris 20 mM pH 7.2, CaCl₂ 10 mM, ZnCl₂ 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.5 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε₂₈₀ = 28420 M^-1cm^-1 calculated).

Specific activity
> 80 U/μg. Activity described as U=100 pmol/min at 25°C using a colorimetric assay with thiopeptide Ac-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC₂H₅ (Biomol) as substrate.

Storage
-80°C. After initial defrost, aliquot the product into individual tubes and refreeze at -80°C.
Avoid repeated freeze/thaw cycles.

Usage
Enzyme kinetic studies, cleavage of target substrates and screening of inhibitors.

Releted research fields

• Biomaterials
• Dental diseases
  • caries
  • periodontitis
• Osteoarthritis
• Wound healing

Bode, W. et al. Cell. Mol. Life Sci. 55 (4), 639-652 (1999).
Betz, M. et al. Eur. J. Biochem. 247 (1), 356-363 (1997).
Murphy, G. & Knäuper, V. Matrix Biol. 15 (8-9), 511-518 (1997).
Ho, T.F. et al. Gene 146 (2), 297-301 (1994).