Cathepsin D is a ubiquitously expressed lysosomal protease that is involved in proteolytic degradation, cell invasion, and apoptosis. It is suspected to play important roles in protein catabolism, antigen processing, degenerative diseases, and cancer progression. Cathepsin D is present in many types of cancer cells. In breast cancer, it is induced by estrogens and its expression is correlated with a higher risk of metastasis and poor disease-free survival. Extensive studies have been also performed to evaluate the clinical and therapeutic implication of Cathepsin D expression in nongynecological solid tumors. Although conflicting results have been observed in some reports, evidence emerging from these studies indicated that Cathepin D seems to facilitate early stages of tumor progression such as cell proliferation and local dissemination. (Shipping Cost: €200.00)

Fibronectin [IST-9]

Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.

Fibronectin [IST-9]