Anti-MMP1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Matrix metalloproteinase-1 (MMP-1), also known as interstitial collagenase and fibroblast collagenase, is an enzyme that in humans is encoded by the MMP1 gene. MMP-1 was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA. 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. This gene encodes a secreted enzyme which breaks down the interstitial collagens, types I, II, and III. It is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants. Protein function: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. [The UniProt Consortium]