MMP10
MMP10 (matrix metallopeptidase 10, also known as stromelysin-2 or STMY2) is a secreted member of the M10 family of matrix metalloproteinases. It degrades extracellular matrix components, including fibronectin and gelatins, and activates procollagenase. Browse Assay Genie's current range of MMP10 research reagents below, or read on for the biology behind the target.
MMP10 is a secreted protease that acts in the extracellular space and extracellular matrix. It can degrade fibronectin and gelatins of types I, III, IV and V, and weakly degrades collagens III, IV and V. NCBI Gene also lists laminin, elastin and proteoglycan core protein among its substrates. MMP10 additionally activates procollagenase, so it can influence matrix turnover indirectly as well as directly.
The MMP10 gene encodes a preproprotein that is proteolytically processed to generate the mature protease. The protein belongs to the peptidase M10A family and to the HGNC group of M10 matrix metallopeptidases. The gene sits within a cluster of MMP genes on chromosome 11. Mouse and rat both carry an orthologous Mmp10 gene, which allows the enzyme to be studied in common rodent models. Researchers looking for an MMP10 antibody, MMP10 ELISA kit or MMP10 protein will usually be studying matrix degradation in these settings.
Proteins in the MMP family take part in the breakdown of extracellular matrix in normal physiological processes, including embryonic development, reproduction and tissue remodelling. They are also involved in disease processes such as arthritis and metastasis. The protein has also been called stromelysin-2, and earlier gene names include matrix metalloproteinase 10 (stromelysin 2) and the symbol STMY2. Its close relatives in the family include MMP-3, the other stromelysin, and the collagenases that MMP10 activates.
MMP10 degrades fibronectin, gelatins and several collagens, making it a relevant protease for studying matrix breakdown and tissue remodelling.
MMP family members take part in matrix turnover during embryonic development and reproduction, which frames the study of MMP10 in these processes.
Matrix metalloproteinases are implicated in arthritis, so MMP10 is studied as part of the protease activity that degrades joint matrix.
MMP10 activates procollagenase and belongs to a family linked to metastasis, supporting work on matrix protease cascades.
MMP10 is a secreted matrix metalloproteinase that degrades extracellular matrix. It cleaves fibronectin and gelatins of types I, III, IV and V, and weakly cleaves collagens III, IV and V. It also activates procollagenase, adding an indirect route to matrix turnover.
MMP10 is also called stromelysin-2, the UniProt protein name, and STMY2. Earlier HGNC names were matrix metalloproteinase 10 (stromelysin 2) and stromelysin 2. The enzyme carries EC number 3.4.24.22 and belongs to the peptidase M10A family.
Yes. Both mouse and rat have an orthologous gene named Mmp10, so the protease can be studied in rodent models. Human MMP10 lies in a cluster of MMP genes on chromosome 11. Check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases, including stromelysins, collagenases and gelatinases involved in extracellular matrix turnover.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P09238; product specifications from Assay Genie datasheets.