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Details of RareLED ID Assay_1017
Primary information
GENECTSS
NUMBER OF ASSAY157
ASSAY IDs360104 273239 747795 257088 255215 387651 1169036 364996 339651 307164 288393 51529 691903 263487 261376 254423 448877 273240 1257963 361730 271487 270166 240980 219376 717410 609677 609672 609669 493665 493661 484232 51525 367815 266479 257089 51524 746596 493849 473211 255873 51399 1259214 328997 308691 301506 295326 263658 262993 262989 262162 241273 51527 721428 721427 691962 569126 554255 539530 489431 473254 473210 473209 441177 440406 699425 1241506 370547 321240 264539 256978 254762 242535 242162 240724 51530 51523 717412 493403 484233 1299798 51533 569015 493851 473212 314222 301507 268739 256972 242499 242380 1258204 1258149 1257951 1257709 51537 51545 51544 51531 51526 703433 677818 569154 539535 526074 489432 473255 466515 470231 441178 430245 428165 1344626 1344175 310232 308313 277534 242865 1168919 570626 493407 466814 1322990 365201 314233 293185
Assay Name1. Inhibition of human recombinant cathepsin S after 10 mins,2. Inhibition of cathepsin S,3. Inhibition of human cathepsin-S,4. Inhibitory activity against human cathepsin S,5. Apparent inhibitory constant against human cathepsin S,6. Inhibition of human recombinant cathepsin S by fluorometric assay,7. Inhibition of human cathepsin S using benzyloxycarbonyl-L-Leucyl-L-Arginine 4-Methyl-coumaryl-7-amide substrate by FRET assay,8. Inhibition of human recombinant cathepsin S by fluorescence assay,9. Inhibition of human recombinant cathepsin S by fluorescence assay,10. Inhibition of cathepsin S,11. Inhibition of cathepsin S,12. Equilibrium dissociation constant determined using fluorescence based competitive binding assay towards Cathepsin S,13. Inhibition of human cathepsin S using Z-Phe-Val-Arg-pNA as substrate after 80 mins by spectrophotometric analysis,14. Inhibition of Cathepsin S,15. Inhibition of human cathepsin S,16. Inhibitory concentration against recombinant human Cathepsin S at 37 degree C at pH 5.5,17. Inhibition of cathepsin S after 10 to 15 mins by fluorescence assay,18. Binding affinity to cathepsin S,19. Enzyme Assay: The assay uses baculovirus-expressed human cathepsin S and the boc-Val-Leu-Lys-AMC fluorescent substrate available from Bachem in a 384 well plate format, in which 7 test compounds can be tested in parallel with a positive control comprising a known cathepsin S inhibitor comparator. The first test compound prepared in DMSO is added to column 1 of the top row, typically at a volume to provide between 10 and 30 times the initially determined rough K. The rough Ki is calculated from a preliminary run in which 10 inverted question markl/well of 1 mM boc-VLK-AMC (1/10 dilution of 10 mM stock in DMSO diluted into assay buffer) is dispensed to rows B to H and 20 inverted question markl/well to row A of a 96 well Microfluor plate. 2 inverted question markl of each 10 mM test compound is added to a separate well on row A, columns 1-10. Add 90 inverted question markl assay buffer containing 1 mM DTT and 2 nM cathepsin S to each well of rows B-H and 180 inverted question markl ,20. Inhibition of human recombinant cathepsin S by fluorometric assay,21. Inhibition of cathepsin S,22. Inhibition of Cathepsin S,23. Inhibitory concentration against cathepsin S,24. Inhibitory activity against Human cathepsin S,25. Inhibition of cathepsin S-mediated antigen presentation in B/T hybridoma cells assessed as IL-2 level,26. Inhibition of cathepsin S in human Raji cells assessed as decrease in cell surface expression of MHC class 2/CLIP by flow cytometric analysis,27. Inhibition of human recombinant cathepsin S using Ac-KQLR-AMC as substrate by fluorescence assay,28. Inhibition of human cathepsin S using Z-Lys-Gln-Lys-Leu-Arg-AMC as substrate after 1 hr by fluorescence assay,29. inhibition of cathepsin S in human JY cells assessed as Lip10 accumulation by Western blotting,30. Inhibition of human recombinant cathepsin S,31. Inhibition of cathepsin S in human B cells,32. Inhibitory activity against recombinant human cathepsin S (cat S) expressed in baculovirus,33. Inhibition of human recombinant cathepsin S expressed in baculovirus by fluorescence assay,34. Inhibition of human cathepsin S,35. Inhibitory activity against human cathepsin S expressed in ramos cells,36. Inhibition of recombinant human cathepsin S in a fluorescence assay,37. Inhibition of recombinant cathepsin-S (unknown origin) using Z-Val-Arg-AMC as substrate by fluorescence assay,38. Inhibition of human cathepsin S by fluorescence assay,39. Inhibition of human cathepsin S by ADAM-28 substrate-based fluorescence assay,40. In situ inhibitory concentration against cathepsin in human tissue sections containing osteoclasts,41. In vitro inhibitory activity against human cathepsin S, using 2 uM of Z -Leu-Arg-AMC as substrate,42. In Vitro Inhibition Assay: The inhibitory activity of the compounds of the invention was demonstrated in vitro by measuring the inhibition of recombinant human Cathepsin S as follows: To a 384 well microtitre plate is added 10 inverted question markl of a 100 inverted question markM solution of test compound in assay buffer (100 mM sodium acetate pH5.5, 5 mM EDTA, 5 mM dithiothreitol) with 10% dimethylsulfoxide (DMSO), plus 20 inverted question markl of 250 inverted question markM solution of the substrate Z-Val-Val-Arg-AMC (7-amido-coumarine derivative of the tripeptide N-benzyloxy-carbonyl-Val-Val-Arg-OH) in assay buffer and 45 inverted question markl of assay buffer. 25 inverted question markl of a 2 mg/l solution of activated recombinant human cathepsin S, in assay buffer, is then added to the well, yielding a final inhibitor concentration of 10 inverted question markM.Enzyme activity is determined by measuring the fluorescence of the liberated aminomethylcoumarin at 440 nM ,43. Inhibition of human recombinant cathepsin S by fluorescence assay,44. Inhibition of human cathepsin S,45. Inhibition of human cathepsin S,46. Inhibition of human cathepsin S,47. Inhibition of cathepsin S,48. Inhibition of Cathepsin S,49. Potency against Cathepsin S in Ramos cells by whole cell enzyme occupancy assay,50. Inhibition of cathepsin S,51. Inhibitory concentration against human cysteine protease cathepsin S,52. Inhibitory concentration against human recombinant Cathepsin S expressed in baculovirus,53. Inhibition of human cathepsin S,54. Inhibition of cathepsin S in human JY cells assessed as invariant chain-li degradation,55. Inhibition of human cathepsin S using Z-Phe-Val-Arg-pNA as substrate after 10 mins by spectrophotometric analysis,56. Inhibition of human cathepsin S,57. Inhibition of human cathepsin S after 30 mins by spectrophotometric assay,58. Inhibition of human cathepsin S by fluorescence assay,59. Inhibition of cathepsin S-mediated invariant chain degradation in human JY B-cells assessed as accumulation of p10 fragment by Western blot analysis,60. Inhibition of human recombinant cathepsin S expressed in baculovirus expression sytem after 15 mins by FRET assay,61. Inhibition of cathepsin S in human JY cells assessed as inhibition of invariant chain degradation,62. Inhibition of human cathepsin S,63. Inhibition of human recombinant cathepsin S expressed in baculovirus by FRET assay,64. Inhibition of human recombinant cathepsin S expressed in baculovirus by FRET assay,65. Inhibition of human recombinant CatS assessed as suppression of enzyme-mediated Z-Val-Val-Arg-AMC cleavage by QFRET assay,66. Inhibition of human cathepsin-S using Z-Phe-Val-Arg-AMC as substrate preincubated for 30 mins measured after 10 mins by fluorescence assay,67. Inhibition of human recombinant cathepsin S by fluorescence assay,68. Inhibition of human recombinant cathepsin S,69. Inhibition of cathepsin S,70. Inhibitory constant against human cathepsin S using Z-Val-Val-Arg-AMC substrate,71. Inhibitory activity against cathepsin S from human,72. Inhibitory concentration against human cathepsin S by fluorescence assay using 10 uM Cbz-Val-Val-Arg-AMC,73. Inhibition of 10 uM Cbz-Val-Val-Arg-AMC binding to human cathepsin S in fluorescence assay,74. Inhibitory concentration against human cathepsin S,75. Binding affinity of compound was evaluated against cathepsin S.,76. Inhibition of recombinant human cathepsin S,77. Inhibition of cathepsin S using FR-aminoluciferin as substrate preincubated for 15 mins before substrate addition measured after 1 hr by luminescence assay,78. Inhibition of human cathepsin S by fluorescence assay,79. Inhibition of human recombinant cathepsin S expressed in Escherichia coli BL21 (DE3) after 10 mins by fluorescence assay,80. Inhibition of human recombinant cathepsin S using Cbz-Phe-Arg-AMC as substrate incubated for 60 mins measured for 20 mins by spectrofluorometrical analysis,81. Inhibition of human Cathepsin S,82. Activity at recombinant cathepsin S,83. Inhibition of cathepsin S-mediated proteolytic cleavage of MHC2 associated invariant chain in human JY cells assessed as accumulation of lip10 by Western blot analysis,84. Inhibition of cathepsin S in human JY cells assessed as accumulation of invariant chain p10 fragment after 24 hrs by Western blot analysis,85. Inhibition of cathepsin S,86. Inhibition of cathepsin S in human JY cells by invariant chain degradation assay,87. Inhibition of human cathepsin S,88. Inhibitory activity against human cathepsin S using Z-Val-Val-Arg-NHMec substrate,89. Inhibition of 10 lM Cbz-Val-Val-Arg-AMC binding to human cathepsin S in fluorescence assay with 100 mM NaOAc,90. Inhibitory concentration against recombinant human cathepsin S by using Z-Leu-Leu-Arg-AMC as synthetic substrate,91. Enzyme Inhibition Assay: Enzyme activity is measured by observing the increase in fluorescence intensity caused by cleavage of a peptide substrate containing a fluorophore whose emission is quenched in the intact peptide.Assay buffer: 100 mM potassium phosphate pH 6.5, EDTA-Na 5 mM, Triton X-100 0.001%, DTT 5 mM.Enzymes (all at 1 nM): human and mouse Cathepsin S, Cat K, Cat B, Cat L.Substrate (20 inverted question markM): Z-Val-Val-Arg-AMC, except for Cat K which uses Z-Leu-Arg-AMC (both from Bachem).Z=Benzyloxycarbonyl.AMC=7-Amino-4-Methyl-Coumarin.DTT=dithiothreitol.Final volume: 100 inverted question markL.Excitation 360 nm, Emission 465 nm.Enzyme is added to the substance dilutions in 96-well microtitre plates and the reaction is started with substrate. Fluorescence emission is measured over 20 minutes, during which time a linear increase is observed in the absence of inhibitor.,92. Inhibition Assay: Enzyme activity is measured by observing the increase in fluorescence intensity caused by cleavage of a peptide substrate containing a fluorophore whose emission is quenched in the intact peptide. Assay buffer: 100 mM potassium phosphate pH 6.5, EDTA-Na 5 mM, Triton X-100 0.001%, DTT 5 mM. Enzymes (all at 1 nM): human and mouse Cathepsin S, Cat K, Cat B, Cat L. Substrate (20 inverted question mar
ACTIVITYSubstance BioActivity: 8 Active, 1 Activity <= 1 nM, 5 Activity <= 1 µM, 12 Tested Substance BioActivity: 5 Active, 4 Activity <= 1 µM, 5 Tested Substance BioActivity: 28 Active, 31 Activity <= 1 µM, 31 Tested Substance BioActivity: 4 Active, 1 Activity <= 1 µM, 6 Tested Substance BioActivity: 9 Active, 2 Activity <= 1 nM, 9 Activity <= 1 µM, 9 Tested Substance BioActivity: 11 Active, 12 Activity <= 1 µM, 12 Tested Substance BioActivity: 5 Active, 2 Activity <= 1 µM, 5 Tested Substance BioActivity: 8 Active, 8 Activity <= 1 µM, 8 Tested Substance BioActivity: 29 Active, 30 Activity <= 1 µM, 30 Tested Substance BioActivity: 34 Active, 29 Activity <= 1 µM, 38 Tested Substance BioActivity: 4 Active, 1 Activity <= 1 nM, 4 Activity <= 1 µM, 4 Tested Substance BioActivity: 26 Active, 15 Activity <= 1 nM, 26 Activity <= 1 µM, 27 Tested Substance BioActivity: 1 Active, 1 Activity <= 1 nM, 1 Activity <= 1 µM, 1 Tested Substance BioActivity: 26 Active, 1 Activity <= 1 nM, 25 Activit