Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | it is shown that hepatocyte growth factor activator inhibitor type-1 is not required for activation of matriptase in stably transfected Madin-Darby canine kidney cells | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
full-length rat matriptase is expressed with a myc-epitope and a hexahistidine tag at its C-terminus in stably transfected Madin-Darby canine kidney cells | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Aprotinin | - |
Rattus norvegicus | |
hepatocyte growth factor activator inhibitor type-1 | - |
Rattus norvegicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
Western blot analysis using conditioned medium, catalytic domain of proteolytically active two-chain matriptase C-terminal fragment | Rattus norvegicus |
90000 | - |
Western blot analysis using conditioned medium, proteolytically inactive single-chain C-terminal fragment | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | matriptase is processed post-translationally via cleavage between Gly149 and Ser150. The C-terminal fragment Ser150-Val855 occurs abundantly in the conditioned medium | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
matriptase | - |
Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
physiological function | hepatocyte growth factor activator inhibitor type-1 is not required for activation of matriptase in stably transfected Madin-Darby canine kidney cells | Rattus norvegicus |