| Identification | Back Directory | [Name]
DABCYL-LEU-ALA-GLN-ALA-VAL-ARG-SER-SER-SER-ARG-EDANS | [CAS]
396716-14-6 | [Synonyms]
TACE FRET Substrate I
TACE FRET SUBSTRATE III
DABCYL-LAQAVRSSSR-EDANS
DABCYL-TNF-α-EDANS (-4 to +6)
TACE SUBSTRATE III, FLUOROGENIC
ADAM-17 SUBSTRATE II, FLUOROGENIC
ADAM-17 SUBSTRATE III, FLUOROGENIC
DABCYL-TNF-a-EDANS: -4 to +6, human
DABCYL-TNF-α-EDANS (-4 to +6) (human)
DABCYL-TNF-α-EDANS (-4 to +6) (human)
DABCYL-TNF-ALPHA-EDANS (-4 TO +6) (HUMAN)
TNF-ALPHA CONVERTASE ENZYME SUBSTRATE, FLUOROGENIC
DABCYL-LEU-ALA-GLN-ALA-VAL-ARG-SER-SER-SER-ARG-EDANS
TNF-ALPHA CONVERTASE ENZYME SUBSTRATE II, FLUOROGENIC
DABCYL-TUMOR NECROSIS FACTOR-ALPHA-EDANS (-4 TO +6) (HUMAN)
DABCYL-TNF-α-EDANS (-4 to +6) (human) trifluoroacetate salt
DABCYL-TNF-alpha-EDANS (-4 to +6) (human) trifluoroacetate salt
L-Argininamide,N-[4-[[4-(dimethylamino)phenyl]azo]benzoyl]-L-leucyl-L-alanyl-L-glutaminyl-L-alanyl-L-valyl-L-arginyl-L-seryl-L-seryl-L-seryl-N-[2-[(5-sulfo-1-naphthalenyl)amino]ethyl]-
L-Argininamide, N-[4-[[4-(dimethylamino)phenyl]azo]benzoyl]-L-leucyl-L-alanyl-L-glutaminyl-L-alanyl-L-valyl-L-arginyl-L-seryl-L-seryl-L-seryl-N-[2-[(5-sulfo-1-naphthalenyl)amino]ethyl]- (9CI) | [Molecular Formula]
C70H104N22O18S | [MDL Number]
MFCD00798779 | [MOL File]
396716-14-6.mol | [Molecular Weight]
1573.78 |
| Chemical Properties | Back Directory | [density ]
1.46±0.1 g/cm3(Predicted) | [storage temp. ]
-15°C | [solubility ]
50% acetic acid: 5mg/mL
DMSO: 5mg/mL | [form ]
lyophilized solid | [pka]
-0.26±0.40(Predicted) | [color ]
red | [Sequence]
{DABCYL}-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-{EDANS} |
| Hazard Information | Back Directory | [Uses]
DABCYL-TNF-α-EDANS (-4 to +6) (human) is a FRET peptide substrate of tumor necrosis factor convertase (TACE)[1]. | [Biological Activity]
Cell permeable: no''Km = 19 μM as a fluorescence resonance energy transfer (FRET) peptide substrate for TACE''Primary Target
A fluorescence resonance energy transfer (FRET) peptide substrate for TACE''Product does not compete with ATP.''Reversible: no | [References]
[1] Liepinsh E, et al. NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding. J Biol Chem. 2003 Jul 11;278(28):25982-9. DOI:10.1074/jbc.M302734200 |
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