Anti-MMP10 Antibody Picoband® Fluoro647 Conjugated

Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene. 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. The enzyme encoded by this gene degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.

E. coli-derived human MMP10 recombinant protein (Position: Y239-C476) . Human MMP10 shares 74.4% and 73.9% amino acid (aa) sequence identity with mouse and rat MMP10, respectively.

Angiogenesis, Cancer, Cardiovascular, Cell Biology, ECM Enzymes, Extracellular Matrix, Invasion/Microenvironment, Metalloprotease, Proteolysis/Ubiquitin, Proteolytic Enzymes

1. Jung JY, Warter S, Rumpler Y (1990) . Localization of stromelysin 2 gene to the q22.3-23 region of chromosome 11 by in situ hybridization. Ann. Genet. 33 (1) : 21–3. 2. Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988) . The collagenase gene family in humans consists of at least four members. Biochem. J. 253 (1) : 187–92.