MMP-9
MMP-9 (matrix metallopeptidase 9, also known as gelatinase B, 92kDa type IV collagenase and CLG4B) is a secreted matrix metalloproteinase that degrades components of the extracellular matrix. It has an essential role in local proteolysis and in leukocyte migration. Browse Assay Genie's current range of MMP-9 research reagents below, or read on for the biology behind the target.
MMP-9 is a matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. It cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments, and it degrades fibronectin but not laminin or Pz-peptide. It also cleaves KiSS1 at a Gly-|-Leu bond and cleaves NINJ1 to generate the secreted form of ninjurin-1. It could also play a role in bone osteoclastic resorption.
The MMP9 gene encodes a protein of the peptidase M10A family, and HGNC places it in the M10 matrix metallopeptidases group and the elastases. Like most MMPs, it is secreted as an inactive proprotein that is activated when cleaved by extracellular proteinases. The mature enzyme is found in the extracellular space and extracellular matrix. Mouse and rat each have an orthologous Mmp9 gene, so the enzyme can be studied in common rodent models.
The MMP family is involved in breakdown of the extracellular matrix during normal processes such as embryonic development, reproduction and tissue remodelling, and in disease processes such as arthritis and metastasis. Studies in rhesus monkeys suggest that MMP-9 is involved in IL-8-induced mobilisation of haematopoietic progenitor cells from bone marrow. Murine studies suggest a role in tumour-associated tissue remodelling. Earlier names for the gene product include matrix metalloproteinase 9, gelatinase B and 92kDa gelatinase, and researchers will see these terms in older literature on the MMP-9 protein.
MMP-9 degrades type IV and V collagens and fibronectin, making it a key enzyme for studying local proteolysis of the extracellular matrix.
MMP-9 has an essential role in leukocyte migration, so it is relevant to work on how immune cells move through tissue.
Studies in rhesus monkeys link MMP-9 to IL-8-induced mobilisation of haematopoietic progenitor cells from bone marrow.
Murine studies suggest MMP-9 contributes to tumour-associated tissue remodelling, and the MMP family is implicated in metastasis and arthritis.
MMP-9 is a secreted matrix metalloproteinase that carries out local proteolysis of the extracellular matrix and supports leukocyte migration. It cleaves type IV and V collagens and degrades fibronectin. It also cleaves KiSS1 and NINJ1, and could play a role in bone osteoclastic resorption.
The HGNC gene symbol is MMP9, with CLG4B as a previous symbol. Earlier names include matrix metalloproteinase 9, gelatinase B, 92kDa gelatinase and 92kDa type IV collagenase. UniProt lists the protein as matrix metalloproteinase-9, with EC number 3.4.24.35.
Yes. Mouse and rat both have an ortholog named Mmp9. Murine studies have suggested a role for the enzyme in tumour-associated tissue remodelling. Check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases and related extracellular matrix-remodelling enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P14780; product specifications from Assay Genie datasheets.