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Literature summary for 3.4.22.B30 extracted from
- Characterization of endogenous and recombinant human calpain-10 (2008), Biochimie, 90, 1362-1371.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HEK-293F cell | - |
Homo sapiens | - |
| HeLa-S3 cell | two major isoforms with intact N-terminus but different C-terminal T domains | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | none of the calpain-10 proteins purified from different sources has putative proteolytic activity under in vitro conditions when examined using different peptide substrates, including more than 70 in vitro translated, radiolabeled oligopeptides. Calpain-10 may require a special intracellular localization or interacting partner(s) to acquire proteolytic activity, or it may functions by interacting with other proteins rather than through its proteolytic activity | Homo sapiens | ? | - |
? |  |
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