Activating Compound | Comment | Organism | Structure |
---|---|---|---|
4-aminophenylmercuric acetate | activation of pro-MMP-9 constructs at pH 7.0 | Mus musculus |
Application | Comment | Organism |
---|---|---|
drug development | MMP-9 is an attractive target for therapeutic intervention studies in mouse models | Mus musculus |
Cloned (Comment) | Organism |
---|---|
expression of wild-type full-length MMP-9 and of a mutant version lacking the O-glycosylated linker region and hemopexin domains in Drosophila melanogaster S2 cells using the Drosophila metallothionein promoter, the native MMP-9 signal peptide is utilized for secretion contained in the beginning of the sequences | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of a mutant version lacking the O-glycosylated linker region and hemopexin domains and containing only the protease domain, residues 1-447 | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme is secreted | Mus musculus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required | Mus musculus | |
Zn2+ | zinc metalloprotease | Mus musculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
82000 | - |
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE | Mus musculus |
92000 | - |
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Gelatin + H2O | Mus musculus | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant activated MMP-9 dimers by gelatin affnity chromatography | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
epidermis | MMP-9 protein is localized at the leading-edge keratinocytes in front of the migrating epidermal layer | Mus musculus | - |
keratinocyte | - |
Mus musculus | - |
macrophage | located within the granulation tissue | Mus musculus | - |
neutrophil | - |
Mus musculus | - |
skin | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Gelatin + H2O | - |
Mus musculus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 60000-65000, extracellular proteolytically active disulfide-linked MMP-9 dimers, SDS-PAGE | Mus musculus |
monomer | 1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE | Mus musculus |
More | MMP-9 is composed of the classical MMP domains including the pro-, catalytic, zinc-binding, and hemopexin domains. MMP-9 contains three fibronectin type II repeats facilitating its binding to collagen. An O-glycosylated linker region unique for MMP-9 connects the protease domain with the hemopexin domains | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
matrix metalloproteinase-9 | - |
Mus musculus |
MMP-9 | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Mus musculus |
General Information | Comment | Organism |
---|---|---|
physiological function | MMP-9 soluble pro-enzyme is implicated in pathological events including cancer invasion. During skin wound healing, MMP-9 is expressed by the migrating leading-edge keratinocytes upon re-epithelialization of the wound | Mus musculus |