5702 Results for: "1-Bromo-4,6-nonadecadiyn"

Supplier: Sheldon Manufacturing

BACTRON chambers are total anaerobic process workstations. Samples can be prepared, cultured, and inspected in the oxygen-free chamber and standard incubator. Unlike anaerobic jars and bags, which unavoidably expose samples to oxygen, BACTRON units provide complete anaerobic environments for all your applications.

Supplier: Genetex

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc-endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hinge region, and a C-terminal hemopexin-like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane-type MMP subfamilies. MMPs contain the motif His-Glu-X-X-His (X represents any amino acid) that binds zinc in the catalytic site, as well as another zinc molecule and two calcium molecules structurally. They fall within the matrixin subfamily and are EC designated 3.4.24.x. This group also contains astacin, reprolysin, and serralysin, as well as other more divergent metalloproteinases. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown.