||Produced in E. coli. Active Matrix Metalloproteinase-11 (MMP-11, Stromelysin-3) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-11 (Phe98-Ser266, NM_005940) with a C-terminal purification tag.
||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 activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP''s, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.
||>95% by SDS-PAGE
||Study enzyme kinetics, cleave target substrates, and screen for inhibitors.
||When stored under the above 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.
||: -70°C. 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. After initial defrost, aliquot product into individual tubes and refreeze at -70°C. Avoid repeated freeze/defrost cycles.