|Cat. No. :
|Product Overview :
||Recombinant Human matrix metalloproteinase-8 (MMP-8, collagenase-2, neurophil collagenase) cloned from human cDNA, expressed inE. coli.The enzyme consists of the catalytic domain of human MMP-8 (residues 105-262 swissprot accession P22894). MW=17.7kDa.
||Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP"s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens.
||> 95% by SDS-PAGE. The enzyme was observed as a single band migrating at a molecular weight of < 20 kDa.
|Specific Activity :
||>80 U/μg. Activity described as U=100 pmol/min at 25ºC using a colorimetric assay with thiopeptolide Ac-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate.
||Enzyme kinetic studies, cleavage of target substrates and screening of inhibitors.
|Supplied As :
||0.2 mg/ml in 20mM Tris, pH 7.2, 10mM CaCl2, 0.1mM ZnCl2, 0.3M NaCl, 0.5M Acetohydroxamic Acid (AHA). The concentration is calculated from the absorbance at 280nm (e280 = 27310 M-1 cm-1).
||Under the above described conditions, to avoid precipitation or protein dimerization, the product can be concentrated to a maximum of 0.5mM.
||-80ºC. The enzyme is stable at -20ºC for at least 1 week. After initial defrost, aliquot enzyme into individual tubes and refreeze at -80ºC. Avoid repeated freeze/defrost cycles.