Recombinant Human MMP28 protein (denatured) is a Human Full Length protein, in the 123 to 520 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Can degrade casein. Could play a role in tissues homeostasis and repair.
MMP25, UNQ1893/PRO4339, MMP28, Matrix metalloproteinase-28, MMP-28, Epilysin
Recombinant Human MMP28 protein (denatured) is a Human Full Length protein, in the 123 to 520 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl
Can degrade casein. Could play a role in tissues homeostasis and repair.
Belongs to the peptidase M10A family.
The precursor is cleaved by a furin endopeptidase.
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.
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.
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.
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15% SDS-PAGE analysis of ab177646 (3μg).
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