MMP-9 human recombinant, expressed in HEK 293 cells, >=95% (SDS-PAGE)

Most MMPs (matrix metalloproteinases) are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases. MMP-9, also known as 92kDa type IV collagenase, 92kDa gelatinase/gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. Structurally, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline rich linker region, and a carboxyl terminal hemopexin like domain.