MMP8
MMP8 (matrix metallopeptidase 8) is a member of the matrix metalloproteinase family, also known as neutrophil collagenase or CLG1. It degrades fibrillar type I, II and III collagens and contributes to extracellular matrix breakdown and tissue remodelling. Browse Assay Genie's current range of MMP8 research reagents below, or read on for the biology behind the target.
MMP8 is a collagenase that can degrade fibrillar type I, II and III collagens. As a member of the matrix metalloproteinase (MMP) family, it takes part in the breakdown of extracellular matrix, a process that underlies embryonic development, reproduction and tissue remodelling. The same proteolytic activity is also involved in disease processes such as arthritis and metastasis. The enzyme is classified as EC 3.4.24.34 and belongs to the peptidase M10A family.
The human MMP8 gene encodes a protein found in cytoplasmic granules and, once secreted, in the extracellular space and extracellular matrix. Proteolysis at different sites on the protein produces multiple active forms of the enzyme with distinct N-termini, and alternative splicing of the gene gives rise to multiple transcript variants. These features mean that the MMP8 protein can exist in several forms, which is worth bearing in mind when designing experiments.
HGNC places the gene in the M10 matrix metallopeptidases group. It sits within a cluster of MMP genes on chromosome 11q22. The approved name, matrix metallopeptidase 8, replaced the earlier name matrix metalloproteinase 8 (neutrophil collagenase), and CLG1 is a previous symbol. Mouse and rat both carry an ortholog named Mmp8, so the enzyme can be studied in common rodent models. MMP8 is often studied alongside other MMP family members, which share the role of matrix turnover but differ in their substrate preferences.
MMP8 degrades fibrillar type I, II and III collagens, making it a focus for studies of collagen turnover.
MMP family proteins break down extracellular matrix during development, reproduction and tissue remodelling, and MMP8 contributes to this activity.
Matrix metalloproteinases such as MMP8 are implicated in disease processes including arthritis, where matrix breakdown is of interest.
The MMP family is linked to metastasis through extracellular matrix degradation, which places MMP8 in cancer biology research.
MMP8, or neutrophil collagenase, is a matrix metalloproteinase that degrades fibrillar type I, II and III collagens. Through this activity it contributes to extracellular matrix breakdown in development, reproduction and tissue remodelling, and in disease processes such as arthritis and metastasis.
MMP8 is also called neutrophil collagenase and CLG1, and was previously named matrix metalloproteinase 8 (neutrophil collagenase). Proteolysis at different sites yields multiple active forms with distinct N-termini, and alternative splicing produces multiple transcript variants.
Yes. Both mouse and rat have an ortholog of the gene, named Mmp8, so the enzyme can be studied in rodent models. Check the datasheet of any product for its validated reactivity.
Other matrix metalloproteinases, including collagenases, gelatinases and stromelysins, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P22894; product specifications from Assay Genie datasheets.