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Details of RareLED ID Assay_1016
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GENECTSO
NUMBER OF ASSAY179
ASSAY IDs370550 367816 367439 365199 364997 361731 342300 358950 358949 339652 339477 328995 321237 314228 314219 310230 308692 308316 308310 307274 307165 293182 290157 290155 288395 277532 273237 271488 270167 268736 266476 264113 263488 262994 262402 262163 262143 261373 260670 259959 259958 257083 256973 255862 255213 254915 254886 254881 254421 242466 242447 242310 242090 241950 240845 240844 240722 240716 240649 239258 238473 238235 219369 219368 219367 219366 51200 51193 51185 51181 51180 51179 51175 51174 48414 48411 48410 48409 48406 48405 48404 48400 48399 48398 48397 51186 51184 51183 51182 51391 1259028 1258375 1258333 1258317 1257962 1257953 1257707 1257706 1257555 1257449 1241503 1230717 1177066 1138572 1118858 51203 51177 48413 48412 48407 48403 219371 51206 51205 51204 51202 51201 51198 51197 51178 51176 48419 48418 48408 48401 1058733 776781 747794 746
Assay Name1. Inhibition of human recombinant cathepsin K by fluorescence assay,2. Inhibition of human recombinant cathepsin K expressed in baculovirus by fluorescence assay,3. Inhibition of humanized rabbit cathepsin K,4. Inhibition of human recombinant cathepsin K by fluorescence assay,5. Inhibition of human recombinant cathepsin K by fluorescence assay,6. Inhibition of human recombinant cathepsin K by fluorometric assay,7. Inhibition of cathepsin K,8. Inhibition of cathepsin K by fluorimetric assay,9. Inhibition of cathepsin K by fluorimetric assay,10. Inhibition of human recombinant cathepsin K by fluorescence assay,11. Inhibition of human recombinant cathepsin K,12. Inhibition of human recombinant cathepsin K by fluorescence assay,13. Inhibition of human recombinant cathepsin K,14. Inhibition of human cathepsin K,15. Inhibition of humanized rabbit cathepsin K,16. Inhibition of cathepsin K by fluorescence assay,17. Inhibition of human cathepsin K,18. Activity of humanized rabbit cathepsin K at 25 uM,19. Inhibition of humanized rabbit cathepsin K,20. Inhibition of humaized rabbit cathepsin K,21. Inhibition of cathepsin K,22. Inhibition of human recombinant cathepsin K,23. Inhibition of human recombinant cathepsin X,24. Inhibition of human recombinant cathepsin K,25. Inhibition of cathepsin K,26. Inhibition of human recombinant cathepsin K,27. Inhibition of cathepsin K,28. Inhibition of cathepsin K,29. Inhibition of Cathepsin K,30. Inhibition of human cathepsin K,31. Inhibition of human cathepsin K,32. Inhibition of recombinant human cathepsin K,33. Inhibition of Cathepsin K,34. Inhibition of humanized rabbit Cathepsin K,35. Inhibition of recombinant human cathepsin K by fluorescence assay,36. Inhibition of cathepsin K,37. Inhibitory activity against recombinant human Cathepsin K,38. Inhibition of human cathepsin K,39. Inhibition of recombinant human cathepsin K in a fluorescence assay,40. Inhibitory activity against human Cathepsin K,41. Inhibitory activity against humanized rabbit Cathepsin K,42. Inhibitory activity against humanized rabbit cathepsin K,43. Inhibitory activity against human cathepsin K using Z-Leu-Arg-NHMec substrate,44. In vitro inhibitory concentration against cathepsin K in cell-based assay of bone resorption,45. Apparent inhibitory constant against human cathepsin K,46. Inhibitory activity against cathepsin K (10 pM) using humanized rabbit enzyme,47. Inhibitory activity against cathepsin K using humanized rabbit enzyme,48. Inhibitory activity against cathepsin K from humanized rabbit enzyme,49. Inhibitory concentration against recombinant human Cathepsin K at 37 degree C at pH 5.5,50. Inhibition of 10 lM Cbz-Phe-Arg-AMC binding to human cathepsin K in fluorescence assay with 100 mM NaOAc,51. Inhibition of 10 uM Cbz-Phe-Arg-AMC binding to human cathepsin K by fluorescence assay,52. Inhibitory concentration against recombinant human cathepsin K by using Z-Phe-Arg-AMC as synthetic substrate,53. Inhibition of 10 uM Cbz-Phe-Arg-AMC binding to human cathepsin K in fluorescence assay,54. Inhibitory concentration against human cathepsin K using 10 uM Cbz-Phe-Arg-AMC,55. Inhibitory potency against human Cathepsin K,56. Inhibitory potency against human Cathepsin K,57. Inhibitory concentration against human cathepsin K,58. Inhibitory concentration against human cathepsin K,59. Inhibition of human cathepsin K,60. Inhibition constant against human cathepsin K in fluorescence assay using Cbz-Phe-Arg-AMC,61. Binding affinity against human cathepsin K,62. Inhibition constant against human cathepsin K,63. Inhibition of Human cathepsin K,64. in vitro cell based assay for measuring the IC50 values of osteoblast resorption.,65. In vitro cell based assay for measuring the IC50 values of osteoblast resorption.,66. In vitro IC50 value was measured using in situ cytochem assay.,67. Eq. constant (Ki) for inhibition of Cathepsin K was determined by progress curves, following hydrolysis of Z-Phe-Arg- Amc in the absence and presence of compound,68. Inhibition of recombinant rabbit Cathepsin K in a fluorescence assay,69. In vitro inhibition of human Cathepsin K.,70. Specificity of Cathepsin K inhibition by the compound,71. Inhibitory constant against human cathepsin K,72. Inhibitory activity tested against human Cathepsin K,73. In vitro inhibitory activity against Human Cathepsin K using 2 uM of Z -Leu-Arg-AMC as substrate,74. Inhibition of Human Cathepsin K,75. Inhibitory constant against human cathepsin K,76. Inhibitory activity tested against Human Cathepsin K using Z-Phe-Arg-pNA as substrate,77. Inhibitory activity tested against Human Cathepsin K receptor using gelatinase assay,78. Inhibitory activity tested against Human Cathepsin K receptor using bone resorption assay,79. Inhibition of recombinant human cathepsin K in fluorescence assay,80. Inhibition of Cathepsin K at pH 7,81. Inhibition of Cathepsin K at pH 5.5,82. In vitro inhibitory activity against human cathepsin K, using 2 uM of Z -Leu-Arg-AMC as substrate,83. Effect of 10 mM of GSH on the inhibitory activity against Cathepsin K, at pH 7,84. Effect of 10 mM of GSH on the inhibitory activity of compound against Cathepsin K, at pH 5.5,85. Concentration required to inhibit 50% of cysteine protease cathepsin K of human,86. Relative binding affinity was measured for Cathepsin K,87. Inhibitory activity measured against cathepsin K.,88. The apparent binding affinity against cathepsin K.,89. Inhibition of cathepsin K,90. Compound is evaluated for inhibitory potency against cathepsin O2,91. Inhibition Assay: To activate the proenzyme, 5 ul procathepsin K were mixed with 1 ul activation buffer, and incubated at room temperature for 30 min.5 uL test compound (final concentration 0.1 nM to 100 uM) in aqua bidest (containing 4% DMSO, final DMSO concentration 1%) were mixed with 10 uL of Cathepsin K in assay buffer (final concentration 2 ng/uL) and incubated for 10 min. Then 5 uL of substrate in assay buffer (final concentration 12.5 uM) were added. The plates were then incubated at room temperature for 60 min. Then, the reaction was stopped by adding 10 uL of E64 in assay buffer (final concentration 1 uM). The fluorescence in the wells was determined using a Molecular Devices SpectraMax M5 Fluorescence Reader (Ex 360 nm, Em 460 nm).Each assay microtiter plate contains wells with vehicle controls (1% DMSO in bidest) as reference for non-inhibited enzyme activity (100% Ctl; high values) and wells with inhibitor (E64 in bidest+1% DMSO.,92. Inhbition Assay: The recombinant human DPPI was diluted in TAGZyme buffer to 1 U/ml (38.1 ug/ml, respectively), and then activated by mixing in a 1:2 ratio with a Cysteamine aqueous solution (2 mM) and incubating for 5 min at room temperature.Five uL test compound (final concentration 0.1 nM to 100 uM) in aqua bidest (containing 4% DMSO, final DMSO concentration 1%) were mixed with 10 uL of DPPI in MES buffer (final concentration 0.0125 ng/uL) and incubated for 10 min. Then, 5 uL of substrate in MES buffer (final concentration 50 uM) were added. The microtiter plates were then incubated at room temperature for 30 min. Then, the reaction was stopped by adding 10 uL of Gly-Phe-DMK in MES-buffer (final concentration 1 uM). The fluorescence in the wells was determined using a Molecular Devices SpectraMax M5 Fluorescence Reader (Ex 360 nm, Em 460 nm) or an Envision Fluorescence Reader (Ex 355 nm, Em 460 nm).,93. Biological Assay: Recombinant human procathepsin K was obtained from Enzo Life Sciences. Activation of the proenzyme was performed in 32.5 mM sodium acetate pH 3.5, EDTA 1 mM, NaCl 500 mM, human procathepsin K 5.5 uM, at room temperature. Activation times were optimized and varied between 35 and 150 minutes. Cathepsin K was preincubated with test compounds at various concentrations for 5 minutes at 25C. The assay was initiated by addition of substrate Z-Phe-Arg-aminomethylcoumarin ("Z-F-R-AMC" Bacchem) and the final assay conditions were 1.5 nM cathepsin K, 50 uM Z-F-R-AMC, 150 mM sodium acetate pH 5.5, 2.5 mM EDTA (Omnipure), 2.5 mM DTT (EMD), 0.01% BRIJ 35 (Sigma), and 4.0% DMSO (Acros). Test compounds were serially diluted with DMSO and water to include a final concentration range of 10 uM to 10 pM. The reaction was monitored fluorometrically for 5 minutes at 25C. using black 96-well Corning 3686 assay microplates with a Thermo Fluoroskan Ascent FL microplate reader.,94. Inhibition Assay: The following buffers were used: Activation buffer: 32.5 mM sodium acetate, adjusted to pH 3.5 with HCl; Assay buffer: 150 mM sodium acetate, 4mM EDTA, 20 mM L-Cysteine, adjusted to pH 5.5 with HCl,Assay conditions: To activate the proenzyme, 5 uLprocathepsin K were mixed with 1 ul activation buffer, and incubated at room temperature for 30 min. 5 uL test compound (final concentration 0.1 nM to 100 uM) in aqua bidest (containing 4% DMSO, final DMSO concentration 1%) were mixed with 10 uL of Cathepsin K in assay buffer (final concentration 2 ng/uL) and incubated for 10 min. Then 5 uL of substrate in assay buffer (final concentration 12.5 uM) were added. The plates were then incubated at room temperature for 60min. Then, the reaction was stopped by adding 10 uL of E64 in assay buffer (final concentration 1 uM). The fluorescence in the wells was determined using a Molecular Devices SpectraMax M5 Fluorescence Reader.,95. Enzyme Assay: Standard assay conditions for the determination of kinetic constants used a fluorogenic peptide substrate, typically H-D-Ala-Leu-Lys-AMC, and were determined in either 100 mM Mes/Tris, pH 7.0 containing 1 mM EDTA and 10 mM 2-mercaptoethanol or 100 mM Na phosphate, imM EDTA, 0.1% PEG4000 pH 6.5 or 100 mM Na acetate, pH 5.5 containing 5 mM EDTA and 20 mM cysteine, in each case optionally with 1M DTT as stabiliser. The enzyme concentration used was 5 nM. The stock substrate solution was prepared at 10 mM in DMSO. Screens were carried out at a fixed substrate concentration of 60 inverted question markM and detailed kinetic stud
ACTIVITYSubstance BioActivity: 3 Active, 2 Activity <= 1 µM, 3 Tested Substance BioActivity: 47 Active, 32 Activity <= 1 µM, 47 Tested Substance BioActivity: 25 Active, 2 Activity <= 1 nM, 25 Activity <= 1 µM, 25 Tested Substance BioActivity: 4 Active, 4 Activity <= 1 nM, 4 Activity <= 1 µM, 4 Tested Substance BioActivity: 5 Active, 4 Activity <= 1 µM, 8 Tested Substance BioActivity: 11 Active, 12 Activity <= 1 µM, 14 Tested Substance BioActivity: 4 Active, 4 Activity <= 1 nM, 5 Activity <= 1 µM, 5 Tested Substance BioActivity: 2 Active, 2 Tested Substance BioActivity: 3 Active, 3 Activity <= 1 µM, 3 Tested Substance BioActivity: 12 Active, 2 Activity <= 1 nM, 24 Activity <= 1 µM, 28 Tested Substance BioActivity: 8 Active, 1 Activity <= 1 nM, 8 Activity <= 1 µM, 8 Tested Substance BioActivity: 15 Active, 15 Activity <= 1 µM, 15 Tested Substance BioActivity: 20 Active, 2 Activity <= 1 nM, 14 Activity <= 1 µM, 20 Tested Substance BioActivity: 3 Active, 3 Activity <= 1 nM, 3 Activity