Recombinant Human MMP28 protein (GST tag N-Terminus)

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

MMP28 also known as epilysin is a member of the matrix metalloproteinase family. It weighs approximately 53 kDa. This protein is primarily expressed in skin keratinocytes placenta and testis tissues. MMP28 functions mechanically as a protease responsible for the degradation of extracellular matrix components. Its regulation can impact tissue remodeling wound repair and maintenance of homeostasis in the skin and other tissues.

Biological function summary

Matrix metalloproteinase-28 (MMP28) contributes to the dynamic restructuring of tissues. Epilysin is not known to be part of a protein complex but interacts closely with other matrix components for effective extracellular matrix modulation. It helps regulate cell migration and proliferation by modifying the surrounding extracellular environment ensuring the precise orchestration of cellular behaviors during developmental and healing processes.

Pathways

The activity of MMP28 aligns importantly with the extracellular matrix degradation pathway and tissue remodeling pathway. Within these pathways MMP28 interacts with other matrix metalloproteinases such as MMP2 and MMP9. Together they participate in breaking down collagen and other matrix proteins facilitating necessary structural alterations in tissues during various biological events.

Researchers have observed MMP28’s involvement in several pathological conditions such as fibrosis and cancer. In the context of fibrosis MMP28's activity relates to irregular tissue remodeling potentially contributing to fibrotic transformation in organs. In cancer elevated MMP28 expression correlates with tumor progression and metastasis where it interacts with collagens and other extracellular matrix components enabling tumor cells to invade and spread. Insights into MMP28's relationships with other proteins like MMP9 can help develop therapeutic strategies targeting its dysregulation in these conditions.