| Reaction Details |
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 | Report a problem with these data |
| Target | Calpain-2 catalytic subunit |
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| Ligand | BDBM50358148 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_788735 (CHEMBL1924666) |
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| IC50 | 280±n/a nM |
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| Citation |  Stuart, BG; Coxon, JM; Morton, JD; Abell, AD; McDonald, DQ; Aitken, SG; Jones, MA; Bickerstaffe, R Molecular modeling: a search for a calpain inhibitor as a new treatment for cataractogenesis. J Med Chem54:7503-22 (2011) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Calpain-2 catalytic subunit |
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| Name: | Calpain-2 catalytic subunit |
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| Synonyms: | CAN2_HUMAN | CANP 2 | CANPL2 | CAPN2 | Calcium-activated neutral proteinase 2 | Calpain 2 | Calpain M-type | Calpain large polypeptide L2 | Calpain-2 (m-Calpain) | Calpain-2 catalytic subunit | Calpain-2 large subunit | Calpain1/2 | M-calpain | Millimolar-calpain | calpain |
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| Type: | Protein |
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| Mol. Mass.: | 79965.18 |
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| Organism: | Homo sapiens (Human) |
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| Description: | n/a |
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| Residue: | 700 |
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| Sequence: | MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGF
KELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEI
LARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSAL
LEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGC
SIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDN
CPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTK
MDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQR
KMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPG
EYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQ
LAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYIL
WTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFD
NFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL
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| BDBM50358148 |
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| n/a |
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| Name | BDBM50358148 |
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| Synonyms: | CHEMBL1921825 |
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| Type | Small organic molecule |
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| Emp. Form. | C26H32FN3O6S |
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| Mol. Mass. | 533.612 |
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| SMILES | CC(C)[C@@H]1NC(=O)[C@H](Cc2ccc(OCCCC[C@H](NC1=O)C=O)cc2)NS(=O)(=O)c1ccc(F)cc1 |r| |
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| Structure | 
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