Monoclonal antibody clone 3B6 recognizes human matrix metalloproteinase 1 (MMP1). MMPs are a large class of zinc dependent catalytic enzymes. They cleave or degrade virtually all components of the extracellular matrix. MMPs are involved in a wide range of processes like tissue remodeling, wound healing, angiogenesis and regulation of inflammatory processes. They are also involved in pathological processes such as rheumatoid arthritis, inflammation, atherosclerosis, tumor growth and metastasis. MMPs are formed as inactive zymogens which must be cleaved to become active. Activated MMPs are inhibited by TIMPs. TIMP and MMP expression and function are tightly regulated in order to contain a balance in proteolysis and proteolysis inhibition. MMP1 or interstitial collagenase is the major type of proteolytic enzyme and can degrade interstitial collagen types I, II, and III, clearing a path for cells to invade matrix barriers and migrate through tissue stroma. The MMP1 gene is located in 11q22 and is translated in a wide variety of cells, such as fibroblasts, macrophages, endothelial and epithelial cells. Genetic polymorphisms and related gene expression in MMP1 may have a pathogenic role. Under normal physiologic conditions levels of MMP1 are low, but in pathological conditions, such as inflammation, there may be dysregulation of MMP1 because the expression of MMP1 is potently up-regulated by cytokines and growth factors.